diff --git a/education/HADDOCK24/RNA-Pol-III-2022/index.md b/education/HADDOCK24/RNA-Pol-III-2022/index.md
index 104f7e62..c7af808a 100644
--- a/education/HADDOCK24/RNA-Pol-III-2022/index.md
+++ b/education/HADDOCK24/RNA-Pol-III-2022/index.md
@@ -448,8 +448,6 @@ Also consider the Predicted aligned error displayed as a matrix.
It should be rather evident that the prediction confidence for C31 is low. As such it does not make sense to use it as is during the modelling.
But since there are a number of detected cross-links for this domain, in particular with the core and the C82 domains, we could consider including peptide fragments around the cross-linked lysines in the modelling.
-This will be illustrated below in [Strategy 1](#strategy-1-modelling-the-complex-corec82c34c31peptides-by-docking-with-cross-links).
-
diff --git a/education/HADDOCK24/RNA-Pol-III-2024/C31-alphafold.png b/education/HADDOCK24/RNA-Pol-III-2024/C31-alphafold.png
new file mode 100644
index 00000000..009b6bb8
Binary files /dev/null and b/education/HADDOCK24/RNA-Pol-III-2024/C31-alphafold.png differ
diff --git a/education/HADDOCK24/RNA-Pol-III-2024/C34-alphafold.png b/education/HADDOCK24/RNA-Pol-III-2024/C34-alphafold.png
new file mode 100644
index 00000000..fcf2d897
Binary files /dev/null and b/education/HADDOCK24/RNA-Pol-III-2024/C34-alphafold.png differ
diff --git a/education/HADDOCK24/RNA-Pol-III-2024/C82-C34_PAE-alphafold.png b/education/HADDOCK24/RNA-Pol-III-2024/C82-C34_PAE-alphafold.png
new file mode 100644
index 00000000..1821572d
Binary files /dev/null and b/education/HADDOCK24/RNA-Pol-III-2024/C82-C34_PAE-alphafold.png differ
diff --git a/education/HADDOCK24/RNA-Pol-III-2024/C82-alphafold.png b/education/HADDOCK24/RNA-Pol-III-2024/C82-alphafold.png
new file mode 100644
index 00000000..2411c43f
Binary files /dev/null and b/education/HADDOCK24/RNA-Pol-III-2024/C82-alphafold.png differ
diff --git a/education/HADDOCK24/RNA-Pol-III-2024/HADDOCK-result-page.png b/education/HADDOCK24/RNA-Pol-III-2024/HADDOCK-result-page.png
new file mode 100644
index 00000000..aa88a218
Binary files /dev/null and b/education/HADDOCK24/RNA-Pol-III-2024/HADDOCK-result-page.png differ
diff --git a/education/HADDOCK24/RNA-Pol-III-2024/HADDOCK-submission.png b/education/HADDOCK24/RNA-Pol-III-2024/HADDOCK-submission.png
new file mode 100644
index 00000000..d31d400a
Binary files /dev/null and b/education/HADDOCK24/RNA-Pol-III-2024/HADDOCK-submission.png differ
diff --git a/education/HADDOCK24/RNA-Pol-III-2024/Pol-III-architecture.png b/education/HADDOCK24/RNA-Pol-III-2024/Pol-III-architecture.png
new file mode 100644
index 00000000..30b18314
Binary files /dev/null and b/education/HADDOCK24/RNA-Pol-III-2024/Pol-III-architecture.png differ
diff --git a/education/HADDOCK24/RNA-Pol-III-2024/cluster-analysis.png b/education/HADDOCK24/RNA-Pol-III-2024/cluster-analysis.png
new file mode 100644
index 00000000..d6a50685
Binary files /dev/null and b/education/HADDOCK24/RNA-Pol-III-2024/cluster-analysis.png differ
diff --git a/education/HADDOCK24/RNA-Pol-III-2024/core-C82-clashes1.png b/education/HADDOCK24/RNA-Pol-III-2024/core-C82-clashes1.png
new file mode 100644
index 00000000..a6f881d9
Binary files /dev/null and b/education/HADDOCK24/RNA-Pol-III-2024/core-C82-clashes1.png differ
diff --git a/education/HADDOCK24/RNA-Pol-III-2024/core-C82-clashes2.png b/education/HADDOCK24/RNA-Pol-III-2024/core-C82-clashes2.png
new file mode 100644
index 00000000..a5f15b8b
Binary files /dev/null and b/education/HADDOCK24/RNA-Pol-III-2024/core-C82-clashes2.png differ
diff --git a/education/HADDOCK24/RNA-Pol-III-2024/disvis-submission.png b/education/HADDOCK24/RNA-Pol-III-2024/disvis-submission.png
new file mode 100644
index 00000000..dcf218af
Binary files /dev/null and b/education/HADDOCK24/RNA-Pol-III-2024/disvis-submission.png differ
diff --git a/education/HADDOCK24/RNA-Pol-III-2024/graphical-analysis.png b/education/HADDOCK24/RNA-Pol-III-2024/graphical-analysis.png
new file mode 100644
index 00000000..1837e978
Binary files /dev/null and b/education/HADDOCK24/RNA-Pol-III-2024/graphical-analysis.png differ
diff --git a/education/HADDOCK24/RNA-Pol-III-2024/index.md b/education/HADDOCK24/RNA-Pol-III-2024/index.md
new file mode 100644
index 00000000..c8f8afce
--- /dev/null
+++ b/education/HADDOCK24/RNA-Pol-III-2024/index.md
@@ -0,0 +1,1702 @@
+---
+layout: page
+title: "Integrative modelling of the apo RNA-Polymerase-III complex from MS cross-linking and cryo-EM data"
+excerpt: "A tutorial demonstrating the use of MS crosslinks and low resolution cryo-EM data to build a complex molecular machine."
+tags: [MS, Cross-links, cryo-EM, Interaction, HADDOCK, DISVIS, PowerFit, RNA Polymerase, Pymol, Chimera, Visualisation]
+image:
+ feature: pages/banner_education-thin.jpg
+---
+This tutorial consists of the following sections:
+
+* table of contents
+{:toc}
+
+
+
+
+## Introduction
+
+This tutorial will demonstrate the use of our DISVIS, POWERFIT and HADDOCK web servers for predicting the structure of a large biomolecular assembly from MS cross-linking data and low resolution cryo-EM data.
+The case we will be investigating is the apo form of the Saccharomyces cerevisiae RNA Polymerase-III (Pol III). Pol III is a 17-subunit enzyme that transcribes tRNA genes. Its architecture can be subdivided into a core, stalk, heterodimer of C53 and C37, and heterotrimer of C82, C34, and C31 subunits.
+
+
+
+
+Figure 1: Pol III subunits are shown as rectangular bars except for C160 and C128, which are shown as ovals for the sake of clarity. Inter-links are shown as lines connecting the protein bars, while intra-links are shown as curves. Inter-links to C31 are colored yellow, to C34 - gold, to C37 – violet, to C53 - cyan. The remaining inter-links are colored gray. Domains of C82 and C34 discussed in this work are explicitely represented. Regions missing in crystal structures or homology models are colored in black. The figure was created with xiNET. Figure reproduced from Ferber et al, 2016.
+
+
+
+
+During this tutorial, we pretend that the structure of the Pol III core (14 subunits) is known. Therefore, we will focus on modeling the positioning of the C82/C34/C31 heterotrimer subunits relatively to the others (which we will treat as the core of Pol III). The structure of Pol III core is quite well characterized, with multiple cryo-EM structures of Pol III published.
+
+We will be making use of i) our [DISVIS server](https://wenmr.science.uu.nl/disvis/){:target="_blank"} to analyse the cross-links and detect possible false positives and ii) of the new [HADDOCK2.4 webserver](https://wenmr.science.uu.nl/haddock2.4){:target="_blank"} to setup docking runs, using the coarse-graining option to speed up the calculations (especially needed due to the large size of the system).
+As an alternative strategy, we will use our [PowerFit server][link-powerfit-web]{:target="_blank"} to fit the largest components of the complex into the 9Å cryo-EM map and then use those as a starting point for the modelling of the remaining components.
+
+* R.V. Honorato, M.E. Trellet, B. Jiménez-García1, J.J. Schaarschmidt, M. Giulini, V. Reys, P.I. Koukos, J.P.G.L.M. Rodrigues, E. Karaca, G.C.P. van Zundert, J. Roel-Touris, C.W. van Noort, Z. Jandová, A.S.J. Melquiond and **A.M.J.J. Bonvin**. [The HADDOCK2.4 web server: A leap forward in integrative modelling of biomolecular complexes](https://www.nature.com/articles/s41596-024-01011-0.epdf?sharing_token=UHDrW9bNh3BqijxD2u9Xd9RgN0jAjWel9jnR3ZoTv0O8Cyf_B_3QikVaNIBRHxp9xyFsQ7dSV3t-kBtpCaFZWPfnuUnAtvRG_vkef9o4oWuhrOLGbBXJVlaaA9ALOULn6NjxbiqC2VkmpD2ZR_r-o0sgRZoHVz10JqIYOeus_nM%3D). _Nature Prot._, Advanced Online Publication DOI: 10.1038/s41596-024-01011-0 (2024).
+
+Throughout the tutorial, colored text will be used to refer to questions or
+instructions, and/or PyMOL commands.
+
+This is a question prompt: try answering it!
+This an instruction prompt: follow it!
+This is a PyMOL prompt: write this in the PyMOL command line prompt!
+This is a Linux prompt: insert the commands in the terminal!
+
+
+
+## Setup/Requirements
+
+
+In order to follow this tutorial you will need a **web browser**, a **text editor**, [**PyMOL**][link-pymol]{:target="_blank"} and [**Chimera**][link-chimera]{:target="_blank"}
+(both freely available for most operating systems) to visualize the input and output data.
+We used our [**pdb-tools**](https://github.com/haddocking/pdb-tools){:target="_blank"} to pre-process PDB files for HADDOCK,
+renumbering the core domains to avoid overlap in their residue numbering.
+Ready to dock models are provided as part of the material for this tutorial.
+The required data to run this tutorial should be downloaded from [**here**](https://surfdrive.surf.nl/files/index.php/s/hM9IewpGD6dzSad/download){:target="_blank"}.
+Once downloaded, make sure to unpack/unzip the archive (for Windows system you can install the [7-zip](https://www.7-zip.org){:target="_blank"} software if needed to unpack tar archives).
+
+Also, if not provided with special workshop credentials to use the HADDOCK portal, make sure to register in order to be able to submit jobs. Use for this the following registration page: [https://wenmr.science.uu.nl/auth/register/haddock](https://wenmr.science.uu.nl/auth/register/haddock){:target="_blank"}.
+
+
+## HADDOCK general concepts
+
+HADDOCK (see [https://www.bonvinlab.org/software/haddock2.4](https://www.bonvinlab.org/software/haddock2.4){:target="_blank"}) is a collection of python scripts derived from ARIA ([https://aria.pasteur.fr](https://aria.pasteur.fr){:target="_blank"}) that harness the
+power of CNS (Crystallography and NMR System, [http://cns-online.org/v1.3/](http://cns-online.org/v1.3/){:target="_blank"}) for structure
+calculation of molecular complexes. What distinguishes HADDOCK from other docking software is its ability, inherited
+from CNS, to incorporate experimental data as restraints and use these to guide the docking process alongside
+traditional energetics and shape complementarity. Moreover, the intimate coupling with CNS endows HADDOCK with the
+ability to actually produce models of sufficient quality to be archived in the Protein Data Bank.
+
+A central aspect to HADDOCK is the definition of Ambiguous Interaction Restraints or AIRs. These allow the translation
+of raw data such as NMR chemical shift perturbation or mutagenesis experiments into distance restraints that are
+incorporated in the energy function used in the calculations. AIRs are defined through a list of residues that fall
+under two categories: active and passive. Generally, active residues are those of central importance for the
+interaction, such as residues whose knockouts abolish the interaction or those where the chemical shift perturbation is
+higher. Throughout the simulation, these active residues are restrained to be part of the interface, if possible,
+otherwise incurring in a scoring penalty. Passive residues are those that contribute to the interaction, but are of less importance. If such a residue does not belong in the interface there is no scoring penalty. Hence, a
+careful selection of the active and passive residues is critical for the success of the docking.
+
+The docking protocol of HADDOCK was designed so that the molecules experience varying degrees of flexibility and
+different chemical environments, and it can be divided in three different stages, each with a defined goal and
+characteristics:
+
+* **1. Randomization of orientations and rigid-body minimization (it0)**
+In this initial stage, the interacting partners are treated as rigid bodies, meaning that all geometrical parameters
+such as bonds lengths, bond angles, and dihedral angles are frozen. The partners are separated in space and rotated
+randomly about their centers of mass. This is followed by a rigid body energy minimization step, where the partners are
+allowed to rotate and translate to optimize the interaction.
+The role of AIRs in this stage is of particular importance. Since they are included in the energy function being
+minimized, the resulting complexes will be biased towards them. For example, defining a very strict set of AIRs leads
+to a very narrow sampling of the conformational space, meaning that the generated poses will be very similar.
+Conversely, very sparse restraints (e.g. the entire surface of a partner) will result in very different solutions,
+displaying greater variability in the region of binding.
+
+
+
+ See animation of rigid-body minimization (it0):
+
+
+
+
+
+
+
+
+* **2. Semi-flexible simulated annealing in torsion angle space (it1)**
+The second stage of the docking protocol introduces flexibility to the interacting partners through a three-step
+molecular dynamics-based refinement in order to optimize the interface packing. It is worth noting that flexibility in
+torsion angle space means that bond lengths and angles are still frozen. The interacting partners are first kept rigid
+and only their orientations are optimized. Flexibility is then introduced in the interface, which is automatically
+defined based on an analysis of intermolecular contacts within a 5Å cut-off. This allows different binding poses coming
+from it0 to have different flexible regions defined. Residues belonging to this interface region are then allowed to
+move their side-chains in a second refinement step. Finally, both backbone and side-chains of the flexible interface
+are granted freedom.
+The AIRs again play an important role at this stage since they might drive conformational changes.
+
+
+
+ See animation of semi-flexible simulated annealing (it1):
+
+
+
+
+
+
+
+
+* **3. Refinement in Cartesian space with explicit solvent (water)**
+The final stage of the docking protocol allows to immerse the complex in a solvent shell to improve the energetics of the
+interaction. HADDOCK currently supports water (TIP3P model) and DMSO environments. The latter can be used as a membrane
+mimic. In this short explicit solvent refinement the models are subjected to a short molecular dynamics simulation at
+300K, with position restraints on the non-interface heavy atoms. These restraints are later relaxed to allow all side
+chains to be optimized. In the 2.4 version of HADDOCK, the explicit solvent refinement is replaced by default by a simple
+energy minimisation as benchmarking has shown solvent refinement does not add much to the quality of the models. This allows to save time.
+
+
+
+ See animation of refinement in explicit solvent (water):
+
+
+
+
+
+
+
+
+The performance of this protocol depends on the number of models generated at each step. Few models are less
+probable to capture the correct binding pose, while an exaggerated number will become computationally unreasonable. The
+standard HADDOCK protocol generates 1000 models in the rigid body minimization stage, and then refines the best 200
+(ranked based on the HADDOCK score) in both it1 and water. Note, however, that while 1000 models are generated by default
+in it0, they are the result of five minimization trials and for each of these the 180 degrees symmetrical solution is also
+sampled. Thus, the 1000 models written to disk are effectively the sampling results of the 10.000 docking poses.
+
+The final models are automatically clustered based on a specific similarity measure - either the *positional interface
+ligand RMSD* (iL-RMSD) that captures conformational changes about the interface by fitting on the interface of the
+receptor (the first molecule) and calculating the RMSDs on the interface of the smaller partner, or the *fraction of
+common contacts* (current default) that measures the similarity of the intermolecular contacts. For RMSD clustering,
+the interface used in the calculation is automatically defined based on an analysis of all contacts made in all models.
+
+The new 2.4 version of HADDOCK also allows to coarse grain the system, which effectively reduces the number of
+particles and speeds up the computations. We are using for this the [MARTINI2.2 force field](https://doi.org/10.1021/ct300646g){:target="_blank"},
+which is based on a four-to-one mapping of atoms on coarse-grained beads.
+
+
+## The information at hand
+
+Let us first inspect the available data, namely the various structures (or AlphaFold models) as well as
+the information from MS we have at hand to guide the docking. After unpacking the archive provided for this tutorial (see [Setup](#setuprequirements) above),
+you should see a directory called `RNA-Pol-III` with the following subdirectories in it:
+
+ * __cryo-EM__: This directory contains a 9Å cryo-EM map of the RNA Pol III (PolIII_9A.mrc).
+
+ * __disvis__: This directory contains text files called `xlinks-all-X-Y.disvis` describing the cross-links between the various domains (X and Y).
+These files are in the format required to run DISVIS. The directory also containts the results of DISVIS analysis of the various domain pairs as directories named `disvis-results-X-Y`
+
+ * __docking__: This directory contains json files containing all the parameters and input data for HADDOCK. Those are reference files of the docking setup and allow to repeat the modelling using the `Submit File` option of the HADDOCK2.4 web server:
+ * `RNA-PolIII-core-C82-EMfit-C34-C31pept.json`: Docking as described in this tutorial
+
+ * __input-pdbs__: This directory contains the HADDOCK-ready input PDB files for the various domains
+ * `A_PolIII-5fja-core.pdb`: The core region of Pol III with non-overlapping residue numbering (chain A)
+ * `B_C82-alphafold-trimmed.pdb`: The AlphaFold model of C82 excluding the disordered long loops (chain B)
+ * `BE_C82-C34-wHTH3-alphafold-trimmed.pdb`: The AlphaFold-multimer model of C82 and the third helix-turn-helix domain of C34 excluding the disordered long loops (chains B + E)
+ * `C_C34_wHTH1-alphafold.pdb`: The AlphaFold model of the first helix-turn-helix domain of C34 (chain C)
+ * `D_C34_wHTH2-alphafold.pdb`: The AlphaFold model of the second helix-turn-helix domain of C34 (chain D)
+ * `F_C31_alphafold.pdb`: The AlphaFold model of C31 - an unreliable model (chain F)
+ * `F_C31_alphafold-K91-peptide.pdb`: The peptide containing Lysine 91 from C31 AlphaFold model (chain F)
+ * `G_C31_alphafold-K111-peptide.pdb`: The peptide containing Lysine 111 from C31 AlphaFold model (chain G)
+
+ * __restraints__:
+ * `xlinks-all-core-C82-C34-C31-K91-K111.tbl`: This file contains all cross-links between the core, C82, C34 domains
+ and two peptides containing Lys 91 and Lys 111 from the C31 domain (chains F and G, respectively)
+ * `C31-C34-connectivities.tbl`: Connectivity restraints between the C34 domains and between the C31 peptides
+ * `restraints-combined.tbl`: The combination of those two files
+
+* __AF-multimer__:
+ * `C82-C34-wo-template`: AF-multimer run results for predicting C82-C34 binding.
+ * `fasta-seqs`: Fasta sequences for the mobile monomers that can be used for further AF2 modeling.
+
+From MS, we have experimentally determined cross-links between the various domains. We have only kept here the inter-domain cross-links relevant for this tutorial.
+The cross-links are taken from ([Ferber et al. 2016](https://www.nature.com/articles/nmeth.3838){:target="_blank"}. These are the files present in the `disvis` directory. As an example here
+are the cross-links identified between the C82 (chain B here) and C34 (chain C):
+
+
+B 520 CB C 135 CB 0.0 30.0
+B 520 CB C 138 CB 0.0 30.0
+B 520 CB C 141 CB 0.0 30.0
+
From an analysis of the diagonal blocks we can identify the three wHTH domains, whose stucture is well predicted. When considering the off-diagonal blocks, the last domain of C34, wHTH3, seems to be the best defined with respect to C82. We will make use of this in our modelling strategy 2 in this tutorial. Since the orientation of the other domains are not well defined with respect with C82, we will treat them as separate entities during our modelling.
+
+
+
+
+
+
+### C31 AlphaFold model
+
+The C31 AlphaFold model can be accessed [here](https://alphafold.ebi.ac.uk/entry/C7GXV1){:target="\_blank"}.
+
+
+Inspect the 3D model and in particular the color-coding which indicates the model confidence.
+
+
+
+Also consider the Predicted aligned error displayed as a matrix.
+
+
+
+ How much trust to you have in this model?
+
+
+
+
+ See the AlhpaFold model and PAE plot
+
+
+
+
+
+
+
+
+
+
+It should be rather evident that the prediction confidence for C31 is low. As such it does not make sense to use it as is during the modelling.
+But since there are a number of detected cross-links for this domain, in particular with the core and the C82 domains, we could consider including peptide fragments around the cross-linked lysines in the modelling. Two peptide fragments containing respectively K19 and K111 for which cross-links were detected can be found in the `input-pdbs` directory.
+
+
+
+
+## Using DISVIS to visualize the interaction space and filter false positive restraints
+
+
+### Introduction to DISVIS
+
+DisVis is a software developed in our lab to visualise and quantify the information content of distance restraints
+between macromolecular complexes. It is open-source and available for download from our [Github repository][link-disvis]{:target="_blank"}.
+To facilitate its use, we have developed a [web portal][link-disvis-web]{:target="_blank"} for it.
+
+DisVis performs a full and systematic 6 dimensional search of the three translational and rotational degrees of freedom to
+determine the number of complexes consistent with the restraints. It outputs information about the inconsistent/violated
+restraints and a density map that represents the center-of-mass position of the scanned chain consistent with a given
+number of restraints at every position in space.
+
+DisVis requires three input files: atomistic structures of the biomolecules to be analysed and a text file containing the list of distance restraints between the two molecules .
+This is also the minimal required input for the web server to setup a run.
+
+DisVis and its webserver are described in:
+
+* G.C.P. van Zundert, M. Trellet, J. Schaarschmidt, Z. Kurkcuoglu, M. David, M. Verlato, A. Rosato and A.M.J.J. Bonvin.
+[The DisVis and PowerFit web servers: Explorative and Integrative Modeling of Biomolecular Complexes.](https://doi.org/10.1016/j.jmb.2016.11.032){:target="_blank"}.
+_J. Mol. Biol._. *429(3)*, 399-407 (2016).
+
+* G.C.P van Zundert and A.M.J.J. Bonvin.
+[DisVis: Quantifying and visualizing accessible interaction space of distance-restrained biomolecular complexes](https://doi.org/doi:10.1093/bioinformatics/btv333){:target="_blank"}.
+ _Bioinformatics_ *31*, 3222-3224 (2015).
+
+
+### Analysing the Pol III domain-domain interactions with DISVIS
+
+Before modelling Pol III, we will first run DisVis using the cross-links for the various pairs of domains to both
+assess the information content of the cross-links and detect possible false positives. For the latter, please note that DisVis does not account for
+conformational changes. As such, a cross-link flagged as possible false positive might also simply reflect a conformational change occuring upon binding.
+
+We have cross-links available for 9 pairs of domains (see the `disvis` directory from the downloaded data). As an illustration of running DisVis, we will here
+setup the analysis for the Pol III C82 (chain B) - C34 (chain C) pair.
+
+To run DisVis, go to
+
+https://wenmr.science.uu.nl/disvis
+
+On this page, you will find the most relevant information about the server, as well as the links to the local and grid versions of the portal's submission page.
+
+#### Step1: Register to the server (if needed) or login
+
+[Register][link-disvis-register]{:target="_blank"} for getting access to the web server (or use the credentials provided in case of a workshop).
+
+You can click on the "**Register**" menu from any DisVis page and fill the required information.
+Registration is not automatic but is usually processed within 12h, so be patient.
+
+If you already have credential, simply login in the upper right corner of the [disvis input form][link-disvis-submit]{:target="_blank"}
+
+
+#### Step2: Define the input files and parameters and submit
+
+Click on the "**Submit**" menu to access the [input form][link-disvis-submit]{:target="_blank"}.
+
+From the `input-pdbs` directory select:
+
+Fixed chain → B_C82-alphafold-trimmed.pdb
+Scanning chain → C_C34-alphafold-trimmed.pdb
+
+From the `disvis` directory select:
+
+Restraints file → xlinks-C82-C34.disvis
+
+Once the fields have been filled in, you can submit your job to our server
+by clicking on "**Submit**" at the bottom of the page.
+
+If the input fields have been correctly filled you should be redirected to a status page displaying a message
+indicating that your run has been successfully submitted.
+While performing the search, the DisVis web server will update you on the progress of the
+job by reloading the status page every 30 seconds.
+The runtime of this example case is less than 5 minutes on our server using CPUs.
+However the load of the server as well as pre- and post-processing steps might substantially increase the waiting time.
+
+If you want to learn more about the meaning of the various parameters, you can go to:
+
+https://wenmr.science.uu.nl/disvis
+
+Then click on the "**Help/Manual**" menu.
+
+The rotational sampling interval option is in
+degrees and defines how tightly the three rotational degrees of freedom will be
+sampled. Voxel spacing is the size of the grid's voxels that will be cross-correlated during the 3D translational search.
+Lower values of both parameters will cause DisVis to perform a finer search, at the
+expense of increased computational time. The default values are `15°` and `2.0Å` for a quick scanning and `9.72°` and `1.0Å`
+for a more thorough scanning.
+For the sake of time, in this tutorial we will keep the sampling interval as the quick scanning settings (`15.00°` and `2.0Å`).
+The number of processors used for the calculation is fixed to 8 processors on the web server side.
+This number can of course be changed when using the local version of DisVis.
+
+
+#### Analysing the results
+
+Once your job has completed, and provided that you did not close the status page, you will be automatically redirected to the results
+page (you will also receive an email notification).
+
+If you don't want to wait for your run to complete, you can access the pre-calculated results in the data folder you downloaded for this tutorial.
+Look for the `disvis/disvis-results-C82-C34` directly and open in your web browser the `results.html` file present in that directory.
+
+The results page presents a summary split into several sections:
+
+* `Status`: In this section you will find a link from which you can download the output data as well as some information
+about how to cite the use of the portal.
+* `Accessible Interaction Space`: Here, images of the fixed chain together with the accessible interaction space (in
+a density map representation) are displayed. Different views of the molecular scene can be chosen by clicking
+ on the right or left part of the image frame. Each view shows the accessible space consistent with the selected number of restraints (using the slider below the picture).
+* `Accessible Complexes`: Summary of the statistics for the number of complexes consistent with at least N number of restraints.
+ The statistics are displayed for the N levels, N being the total number of restraints provided in the restraints file (here `xlinks-C82-C34.disvis`)
+* `z-Score`: For each restraint provided as input, a z-Score is calculated, indicating the likelihood that a restraint is a false positive.
+The higher the score, the more likely it is that a restraint is a false positive. Putative false positive restraints
+are only highlighted if no single solution was found to be consistent with the total number of restraints provided. If DisVis
+finds complexes consistent with all restraints, the z-Scores are still displayed, but in this case they should be ignored.
+* `Violations`: The table in this sections shows how often a specific restraint is violated for all models consistent with
+a given number of restraints. The higher the violation fraction of a specific restraint, the more likely it is to be a false positive.
+Column 1 shows the number of restraints (N) considered, while each following column indicates the violation fractions of
+a specific restraint for complexes consistent with at least N restraints. Each row thus represents the fraction of all
+complexes consistent with at least N restraints that violated a particular restraint. As for the z-Scores, if solutions are found
+that are consistent with all restraints provided, this table should be ignored.
+
+ Using the different descriptions of the sections we provided above together with the results of your run,
+which ones are the likely false positive restraints according to DisVis?
+
+As mentioned above, the two last sections feature a table that highlights putative false positive restraints based on
+their z-Score and their violation frequency for a specific number of restraints. We will naturally look for the
+crosslinks with the highest number of violations. The DisVis web server preformats the results in a way that false positive restraints
+are highlighted and can be spotted at a glance.
+
+In our case, you should observe that DisVis found solutions consistent with all 3 restraints submitted for C82-C34 interaction.
+
+When DisVis fails to identify complexes consistent with all provided restraints during quick scanning, it is advisable to rerun with the complete scanning parameters before removing all restraints (or removing only the most violated ones and rerunning with complete scanning). It is possible that a more thourough sampling of the interaction space will yield complexes consistent with all restraints or at least reduce the list of putative false positive restraints.
+
+
+
+#### DisVis output files
+
+It is difficult to appreciate the accessible interaction space between the two partners with static images only.
+Therefore you should download the results archive to your computer (which is available at the top of your results page).
+You will find in the archive the following files:
+
+* `accessible_complexes.out`: A text file containing the number of complexes consistent with a number of restraints.
+* `accessible_interaction_space.mrc`: A density file in MRC format. The density represents the space where the center of mass of the
+scanning chain can be placed while satisfying the consistent restraints.
+* `violations.out`: A text file showing how often a specific restraint is violated for each number of consistent restraints.
+* `z-score.out`: A text file giving the z-score for each restraint. The higher the score, the more likely the restraint
+is a false positive.
+* `run_parameters.json`: A text file containing the parameters of your run.
+
+_Note_: Results for the different pair combinations are available from the tutorial data directory in the `disvis` directory as `disvis-results-X-Y`.
+
+Let us now inspect the solutions and visualise the interaction space in Chimera:
+
+
+ Open the *fixed_chain.pdb* file and the *accessible_interaction_space.mrc* density map in Chimera.
+
+
+
+ UCSF Chimera Menu → File → Open... → Select the file
+
+
+Or from the Linux command line:
+
+
+chimera fixed_chain.pdb accessible_interaction_space.mrc
+
+
+The values of the `accessible_interaction_space.mrc` slider bar correspond to the number of satisfied restraints (N).
+In this way, you can selectively visualise regions where complexes have been found to be consistent with a given number of
+restraints. Try to change the level in the "**Volume Viewer**" to see how the addition of restraints reduces
+the accessible interaction space.
+
+_Note_: The interaction space displayed corresponds to the region of space where the center of mass
+ of the scanning molecule can be placed while satisfying a given number of restraints
+
+
+
+ How restrictive are the cross-links in defining the position of C34 around C82? Or put differently: How well-defined in the interaction space around C82?
+
+
+_Remember_ that the displayed interaction space is the region where the center of mass of the second molecule can be put while satistying the distance restraints, contacting and not clashing with the first molecule.
+
+
+
+### Converting DISVIS restraints into HADDOCK restraints
+
+In principle you should repeat the DisVis analysis for all pairs to detect possible false positives.
+For the provided data, however, all cross-links can be satisfied simultaneously, i.e. DISVIS does not identify false positives.
+Before setting up the docking, we need to generate the distance restraint file for the cross-links in a format suitable for HADDOCK.
+HADDOCK uses [CNS][link-cns]{:target="_blank"} as its computational engine. A description of the format for the various restraint types supported by HADDOCK can
+be found in our [Nature Protocols](https://www.nature.com/nprot/journal/v5/n5/abs/nprot.2010.32.html){:target="_blank"} paper, Box 4.
+
+Distance restraints are defined as:
+
+
+
+The lower limit for the distance is calculated as: distance minus lower-bound correction
+and the upper limit as: distance plus upper-bound correction
+
+The syntax for the selections can combine information about chainID - `segid` keyword -, residue number - `resid`
+keyword -, atom name - `name` keyword.
+Other keywords can be used in various combinations of OR and AND statements. Please refer for that to the [online CNS manual][link-cns]{:target="_blank"}.
+
+As an example, a distance restraint between the CB carbons of residues 10 and 200 in chains A and B with an
+allowed distance range between 10 and 20Å can be defined as:
+
+
+assi (segid A and resid 10 and name CB) (segid B and resid 200 and name CB) 20.0 10.0 0.0
+
Additional atoms are included in the distance restraints definitions: `BB`. These correspond to the backbone beads in the MARTINI representation.
+
+
+
+In the restraints directory provided, there is additional restraint file provided: `C31-C34-connectivities.tbl`.
+Inspect its content.
+
+
+What are those restraints for?
+
+
+See solution:
+
+
+
C34 consists of three winged-helix-turn-helix domains which could be docked separately in principle. These are connected by flexible linkers.
+The defined restraints impose upper limits to the distance between the C- and N-terminal domains of the the domains. The upper limit was estimated as the number of missing segments/residues * 4.5Å (a typical distance observed in diffraction data for amyloid fibrils, representing a CA-CA distance in an extended conformation).
+The same applies to C31 for which only two peptide fragments will be used to be able to make use of the cross-link restraints.
+
+
+
+_Note_: You should notice that the restraints are duplicated (actually 4 times). This is a way to tell HADDOCK to give more weight to those restraints.
+
+
+
+
+## Modelling the complex by docking with cross-links only, using as starting conformations the models fitted into the cryo-EM map
+
+We will start by fitting the largest components (core and C82) into the 9Å cryo-EM map using our PowerFit web server.
+This fitted models will then be used as input for the docking with cross-links, keeping those fixed at their original position.
+
+
+
+### Introduction to PowerFit
+
+PowerFit is a software developed in our lab to fit atomic resolution
+structures of biomolecules into cryo-electron microscopy (cryo-EM) density maps.
+PowerFit performs a rigid body fitting, calculating the
+cross-correlation, a common measure of the goodness-of-fit, between the atomic
+structure and the density map. It performs a systematic 6-dimensional scan of
+the three translational and three rotational degrees of freedom. In short,
+PowerFit will try to systematically fit the structure in different orientations at every position
+in the map and calculate a cross-correlation score for each of them.
+
+PowerFit is open-source and available for download from our [Github repository][link-powerfit]{:target="_blank"}.
+To facilitate its use, we have developed a [web portal][link-powerfit-web]{:target="_blank"} for it.
+
+The server makes use of either local resources on our cluster, using the multi-core version of the software, or GPGPU-accelerated grid resources of the
+[EGI](https://www.egi.eu){:target="_blank"} to speed up the calculations. It only requires a web browser to work and benefits from the latest
+developments in the software, based on a stable and tested workflow. Next to providing an automated workflow around
+PowerFit, the web server also summarizes and higlights the results in a single page including some additional postprocessing
+of the PowerFit output using [UCSF Chimera][link-chimera]{:target="_blank"}.
+
+For more details about PowerFit and its usage we refer to a related [online tutorial](/education/Others/powerfit-webserver){:target="_blank"}.
+
+
+### Fitting PolIII-core and C82+C34wHTH3 into the 9Å cryo-EM map
+
+To run PowerFit, go to
+
+https://alcazar.science.uu.nl/services/POWERFIT
+
+On this page, you will find the most relevant information about the server as well as the links to the local and grid versions of the portal's submission page.
+
+Click on the "**Submit**" menu to access the [input form][link-powerfit-submit]{:target="_blank"}:
+
+Complete the form by filling the required fields and selecting the respective files
+(most browsers should also support dragging the files onto the selection button):
+
+Cryo-EM map → PolIII_9A.mrc
+Map resolution → 9.0
+Atomic structure → A_PolIII-5fja-core.pdb
+Rotational angle interval → 10.0
+
+Once the fields have been filled in you can submit your job to our server
+by clicking on "**Submit**" at the bottom of the page.
+
+If the input fields have been correctly filled you should be redirected to a status page displaying a pop-up message
+indicating that your run has been successfully submitted.
+While performing the search, the PowerFit web server will update you on the progress of the
+job by reloading the status page every 30 seconds.
+
+
+For convenience, we have already provided pre-calculated results in the `cryo-EM/powerfit-PolIII-core` directory in the data downloaded for this tutorial.
+The `fit_1.pdb` file corresponds to the top solution predicted by PowerFit. You can inspect it and see how well it fits into the cryo-EM map
+using `Chimera` with its `Volume -> Fit in Map` tool (see instructions above).
+
+
+Repeat the above procedure, but this time for the C82+C34wHTH3 AlphaFold model (`BE_C82-C34-wHTH3-alphafold-trimmed.pdb`).
+Pre-calculated results are available in the `powerfit-PolIII-core/` and `cryo-EM/powerfit-PolIII-C82-C34-wHTH3` directories.
+
+
+
+### Refining the fit in Chimera
+
+Let's see how well did PowerFit perform in fitting and try to further optimize the fit using Chimera.
+
+
+ UCSF Chimera Menu → File → Open... → Select the cryo-EM/powerfit-PolIII-core/fit_1.pdb
+
+
+ UCSF Chimera Menu → File → Open... → Select the cryo-EM/powerfit-PolIII-C82-C34-wHTH3/fit_1.pdb
+
+
+ UCSF Chimera Menu → File → Open... → Select the cryo-EM/PolIII_9A.mrc
+
+
+In the `Volume Viewer` window, the middle slide bar provides control on the
+value at which the isosurface of the density is shown. At high values, the
+envelope will shrink while lower values might even display the noise in the map.
+In the same window, you can click on `Center` to center the view on all visible molecules and the density.
+
+First make the density transparent, in order to be able to see the fitted structure inside:
+
+
+ Within the Volume Viewer window click on the gray box next to Color
+
+
+Set the alpha channel value to around 0.6.
+
+
+In order to distinguish the various chains color the structure by chain:
+
+
+Chimera menu -> Tools -> Depiction -> Rainbow
+Select the option to color by chain and click the Apply button
+
+
+The two molecules were fitted separately into the map, which can cause clashes at the interface.
+Inspect the interface (first turn off the map by clicking on the "eye" in the Volume Viewer window).
+
+
+Can you identify possible problematic areas of the interface?
+
+
+
+See solution:
+
+
There are clearly several regions where the two molecules are clashing.
The fit in chimera has clearly removed some of the chain clashes, but there are still regions where the two molecules are clashing (especially considering we don't visualize the side-chains.
+
+
+
+
+__Note__: In the `cryo-EM` directory of the downloaded data you will find a Python script that can be used to fit a structure into an EM map using Chimera from the command line. Assuming that you are in the pre-calculated`cryo-EM` directory:
+
+
+chimera \-\-nogui \-\-script \"CCcalculate.py PolIII-core-C82-chimera-fitted-CGref.pdb PolIII_9A.mrc 9 10\"
+
+
+The last number in the command is the number of fittings tried from different random positions. The best fit value will be reported.
+
+View an example output of the CCcalculate script:
+
+
+
+RNA-Pol-III-2024/cryo-EM> chimera --nogui --script "CCcalculate.py PolIII-core-C82-C34-wHTH3-chimera-fitted-CGref.pdb PolIII_9A.mrc 9 10"
+Opening PolIII-core-C82-C34-wHTH3-chimera-fitted-CGref.pdb...
+...
+
+Model 0 (PolIII-core-C82-C34-wHTH3-chimera-fitted-CGref.pdb) appears to be a protein without secondary structure assignments.
+Automatically computing assignments using 'ksdssp' and parameter values:
+ energy cutoff -0.5
+ minimum helix length 3
+ minimum strand length 3
+Use command 'help ksdssp' for more information.
+
+Computing secondary structure assignments...
+Computed secondary structure assignments (see reply log)
+reading PolIII_9A.mrc 2.8 Mb 0%
+Done reading PolIII_9A.mrc
+reading PolIII_9A.mrc 178 Mb 0%
+Done reading PolIII_9A.mrc
+Fit 1 of 10
+Fit 2 of 10
+Fit 3 of 10
+Fit 4 of 10
+Fit 5 of 10
+Fit 6 of 10
+Fit 7 of 10
+Fit 8 of 10
+Fit 9 of 10
+Fit 10 of 10
+Fit search: finished
+Found 9 unique fits from 10 random placements having fraction of points inside contour >= 0.100 (10 of 10).
+
+Correlations and times found:
+ 0.952 (1), 0.8203 (1), 0.8133 (1), 0.8103 (2), 0.8049 (1), 0.8041 (1), 0.8009 (1), 0.7976 (1), 0.7753 (1)
+
+Best fit found:
+Fit map molmap PolIII-core-C82-C34-wHTH3-chimera-fitted-CGref.pdb res 9 in map PolIII_9A.mrc using 33394 points
+ correlation = 0.952, correlation about mean = 0.595, overlap = 208
+ steps = 328, shift = 49.3, angle = 31.6 degrees
+Position of molmap PolIII-core-C82-C34-wHTH3-chimera-fitted-CGref.pdb res 9 (#0.1) relative to PolIII_9A.mrc (#1) coordinates:
+ Matrix rotation and translation
+ 0.10322358 -0.51111512 -0.85329141 185.59573168
+ 0.45569008 -0.73824752 0.49733002 190.85526186
+ -0.88413316 -0.44017262 0.15670554 189.33240076
+ Axis -0.69596127 0.02289558 0.71771422
+ Axis point 133.17124957 144.56295228 0.00000000
+ Rotation angle (degrees) 137.65984172
+ Shift along axis 11.08885675
+
+correlation = 0.9496, corr about mean = 0.5599
+Correlation between molmap PolIII-core-C82-C34-wHTH3-chimera-fitted-CGref.pdb res 9 and PolIII_9A.mrc = 0.9496, about mean = 0.5599
+
+
Both cross-links are violated, but especially the one between core residue 5394 and C82 residue 472 (~70Å!).
+The EM fitting solution for C82+C34wHTH3 was well defined according to PowerFit. There seems thus to be discrepancy between the EM and MS data.
+Another explanation could be conformational changes in the structures that are not accounted for in our modelling.
The fit is better than in strategy 1, but thre is still one heavily violated cross-link between resid 472 of C82 and resid 5394 of the core. This might well be a false positive. It was not detected by DISVIS because the analysis is only performed for pair of domain and it can be satisfied, while when considering all molecules and all cross-links it can not.
+
+
+
+
+
+See the best model fit into the EM map:
+
+
+
+
+
+
View of cluster2_4 in the the EM map (correlation 0.9504). C82 and C34 wHTH3 domain (yellow) nicely fit into the density. The other two C34 domains (green and cyan are found in a region where some density starts to appear seen when playing with the density level, which might indicate some disorder / conformational variability.
+
+
+
+
+
+
+## Conclusions
+
+We have demonstrated the use of cross-linking data from mass spectrometry for guiding the docking process in HADDOCK.
+The results show that it is not straightforward to satisfy all cross-links.
+In the original work of [Ferber et al. 2016](https://www.nature.com/articles/nmeth.3838){:target="_blank"} from which the cross-links were taken, many
+cross-links remained violated. See for example Suppl. Table 5 in the corresponding [supplementary material](https://media.nature.com/original/nature-assets/nmeth/journal/v13/n6/extref/nmeth.3838-S1.pdf){:target="_blank"}. It is also possible that the cross-linking experiments might have captured transient or non-native interactions.
+
+Our modelling here was based partially on models (from AlphaFold), which brings another level of complexity. Clearly some domains show much
+more variability in their positions, which might explain why they are not seen in the cryo-EM density.
+
+Using the cryo-EM data to pre-orient molecules prior to docking helps in the modelling of this complex system.
+
+
+
+## Congratulations!
+
+Thank you for following this tutorial. If you have any questions or suggestions, feel free to contact us via email, or post your question to
+our [HADDOCK forum](https://ask.bioexcel.eu/c/haddock){:target="_blank"} hosted by the
+[](https://bioexcel.eu){:target="_blank"} Center of Excellence for Computational Biomolecular Research.
+
+[link-cns]: http://cns-online.org/v1.3/ "CNS online"
+[link-chimera]: https://www.cgl.ucsf.edu/chimera/ "UCSF Chimera"
+[link-disvis]: https://github.com/haddocking/disvis "DisVis GitHub repository"
+[link-disvis-web]: https://wenmr.science.uu.nl/disvis "DisVis web server"
+[link-disvis-submit]: https://wenmr.science.uu.nl/disvis/submit "DisVis submission"
+[link-disvis-register]: https://wenmr.science.uu.nl/auth/register "DisVis registration"
+[link-pymol]: https://www.pymol.org/ "PyMOL"
+[link-haddock]: https://bonvinlab.org/software/haddock2.2 "HADDOCK 2.2"
+[link-haddock-web]: https://wenmr.science.uu.nl/haddock2.4/ "HADDOCK 2.4 webserver"
+[link-haddock-easy]: https://alcazar.science.uu.nl/services/HADDOCK2.2/haddockserver-easy.html "HADDOCK2.2 webserver easy interface"
+[link-haddock-expert]: https://alcazar.science.uu.nl/services/HADDOCK2.2/haddockserver-expert.html "HADDOCK2.2 webserver expert interface"
+[link-haddock-register]: https://wenmr.science.uu.nl/auth/register/"HADDOCK web server registration"
+[link-molprobity]: http://molprobity.biochem.duke.edu "MolProbity"
+[link-powerfit]: https://github.com/haddocking/powerfit "PowerFit"
+[link-powerfit-web]: https://alcazar.science.uu.nl/services/POWERFIT/ "PowerFit web server"
+[link-powerfit-register]: https://wenmr.science.uu.nl/auth/register "PowerFit registration"
+[link-powerfit-submit]: https://alcazar.science.uu.nl/cgi/services/POWERFIT/powerfit/submit "PowerFit submission"
+[link-powerfit-help]: https://alcazar.science.uu.nl/cgi/services/POWERFIT/powerfit/help "PowerFit submission"
+[link-xwalk]: https://www.xwalk.org
diff --git a/education/HADDOCK24/RNA-Pol-III-2024/online-visualisation.png b/education/HADDOCK24/RNA-Pol-III-2024/online-visualisation.png
new file mode 100644
index 00000000..145b52cd
Binary files /dev/null and b/education/HADDOCK24/RNA-Pol-III-2024/online-visualisation.png differ
diff --git a/education/HADDOCK24/RNA-Pol-III-2024/strategy2-EMfit.png b/education/HADDOCK24/RNA-Pol-III-2024/strategy2-EMfit.png
new file mode 100644
index 00000000..63a28286
Binary files /dev/null and b/education/HADDOCK24/RNA-Pol-III-2024/strategy2-EMfit.png differ
diff --git a/education/HADDOCK24/RNA-Pol-III-2024/strategy2-clusters-pymol.png b/education/HADDOCK24/RNA-Pol-III-2024/strategy2-clusters-pymol.png
new file mode 100644
index 00000000..e66d2454
Binary files /dev/null and b/education/HADDOCK24/RNA-Pol-III-2024/strategy2-clusters-pymol.png differ
diff --git a/education/index.md b/education/index.md
index cec6884d..65a07922 100644
--- a/education/index.md
+++ b/education/index.md
@@ -94,7 +94,7 @@ We offer various [research projects](/education/research-projects/) to both bach
* [**Tutorials for DisVis and Powerfit**](/education/Others): Tutorials about rigid-body fitting into cryo-EM maps and assessing the information content of cross-linking data.
-* [**Integrative modelling of the RNA polymerase III apo complex**](/education/HADDOCK24/RNA-Pol-III-2022): A combination of our DISVIS, POWERFIT and HADDOCK2.4 portals using cross-links and cryo-EM data to model a large macromolecular assembly.
+* [**Integrative modelling of the RNA polymerase III apo complex**](/education/HADDOCK24/RNA-Pol-III-2024): A combination of our DISVIS, POWERFIT and HADDOCK2.4 portals using cross-links and cryo-EM data to model a large macromolecular assembly.
* [**2022 BioExcel summerschool metadynamics / HADDOCK tutorial**](/education/biomolecular-simulations-2022)
+
+ 
+ 
+ 
+ 
+ 
+ 
+ 
+
+
+
+
](https://bioexcel.eu){:target="_blank"} Center of Excellence for Computational Biomolecular Research.
+
+[link-cns]: http://cns-online.org/v1.3/ "CNS online"
+[link-chimera]: https://www.cgl.ucsf.edu/chimera/ "UCSF Chimera"
+[link-disvis]: https://github.com/haddocking/disvis "DisVis GitHub repository"
+[link-disvis-web]: https://wenmr.science.uu.nl/disvis "DisVis web server"
+[link-disvis-submit]: https://wenmr.science.uu.nl/disvis/submit "DisVis submission"
+[link-disvis-register]: https://wenmr.science.uu.nl/auth/register "DisVis registration"
+[link-pymol]: https://www.pymol.org/ "PyMOL"
+[link-haddock]: https://bonvinlab.org/software/haddock2.2 "HADDOCK 2.2"
+[link-haddock-web]: https://wenmr.science.uu.nl/haddock2.4/ "HADDOCK 2.4 webserver"
+[link-haddock-easy]: https://alcazar.science.uu.nl/services/HADDOCK2.2/haddockserver-easy.html "HADDOCK2.2 webserver easy interface"
+[link-haddock-expert]: https://alcazar.science.uu.nl/services/HADDOCK2.2/haddockserver-expert.html "HADDOCK2.2 webserver expert interface"
+[link-haddock-register]: https://wenmr.science.uu.nl/auth/register/"HADDOCK web server registration"
+[link-molprobity]: http://molprobity.biochem.duke.edu "MolProbity"
+[link-powerfit]: https://github.com/haddocking/powerfit "PowerFit"
+[link-powerfit-web]: https://alcazar.science.uu.nl/services/POWERFIT/ "PowerFit web server"
+[link-powerfit-register]: https://wenmr.science.uu.nl/auth/register "PowerFit registration"
+[link-powerfit-submit]: https://alcazar.science.uu.nl/cgi/services/POWERFIT/powerfit/submit "PowerFit submission"
+[link-powerfit-help]: https://alcazar.science.uu.nl/cgi/services/POWERFIT/powerfit/help "PowerFit submission"
+[link-xwalk]: https://www.xwalk.org
diff --git a/education/HADDOCK24/RNA-Pol-III-2024/online-visualisation.png b/education/HADDOCK24/RNA-Pol-III-2024/online-visualisation.png
new file mode 100644
index 00000000..145b52cd
Binary files /dev/null and b/education/HADDOCK24/RNA-Pol-III-2024/online-visualisation.png differ
diff --git a/education/HADDOCK24/RNA-Pol-III-2024/strategy2-EMfit.png b/education/HADDOCK24/RNA-Pol-III-2024/strategy2-EMfit.png
new file mode 100644
index 00000000..63a28286
Binary files /dev/null and b/education/HADDOCK24/RNA-Pol-III-2024/strategy2-EMfit.png differ
diff --git a/education/HADDOCK24/RNA-Pol-III-2024/strategy2-clusters-pymol.png b/education/HADDOCK24/RNA-Pol-III-2024/strategy2-clusters-pymol.png
new file mode 100644
index 00000000..e66d2454
Binary files /dev/null and b/education/HADDOCK24/RNA-Pol-III-2024/strategy2-clusters-pymol.png differ
diff --git a/education/index.md b/education/index.md
index cec6884d..65a07922 100644
--- a/education/index.md
+++ b/education/index.md
@@ -94,7 +94,7 @@ We offer various [research projects](/education/research-projects/) to both bach
* [**Tutorials for DisVis and Powerfit**](/education/Others): Tutorials about rigid-body fitting into cryo-EM maps and assessing the information content of cross-linking data.
-* [**Integrative modelling of the RNA polymerase III apo complex**](/education/HADDOCK24/RNA-Pol-III-2022): A combination of our DISVIS, POWERFIT and HADDOCK2.4 portals using cross-links and cryo-EM data to model a large macromolecular assembly.
+* [**Integrative modelling of the RNA polymerase III apo complex**](/education/HADDOCK24/RNA-Pol-III-2024): A combination of our DISVIS, POWERFIT and HADDOCK2.4 portals using cross-links and cryo-EM data to model a large macromolecular assembly.
* [**2022 BioExcel summerschool metadynamics / HADDOCK tutorial**](/education/biomolecular-simulations-2022)