The mechanisms of catalysis and ligand binding for the SARS-CoV-2 NSP3 macrodomain from neutron and X-ray diffraction at room temperature

James Fraser's presentation at the monthly [virtual] Antiviral Drug Discovery (AViDD) Open Science Forum on 19 October 2022. His talk focuses on finding new ligands to the SARS CoV 2 Macrodomain using Fragments, Neutrons, and Entropy.

• Public datasets
  • Identifying new ligands for the SARS-CoV-2 Macrodomain by Fragment Screening and Multi-temperature Crystallography [Interactively explore on Fragalysis]
• Preprints and papers
  • Iterative computational design and crystallographic screening identifies potent inhibitors targeting the Nsp3 Macrodomain of SARS-CoV-2 [DOI]
  • Fragment binding to the Nsp3 macrodomain of SARS-CoV-2 identified through crystallographic screening and computational docking [DOI]
  • The mechanisms of catalysis and ligand binding for the SARS-CoV-2 NSP3 macrodomain from neutron and x-ray diffraction at room temperature [DOI]
  • Of problems and opportunities—How to treat and how to not treat crystallographic fragment screening data [DOI]
• Tutorials
  • Multi-state models from PanDDA
  • Inspecting PanDDA event maps deposited in the Protein Data Bank
• Software
  • Fragmentstein X-ray fragment merging ligand design tools

You can find a recording of his talk on the AViDD Open Science Forum Youtube page

James Fraser is a member of the QBI Coronavirus Research Group (QCRG) AViDD Center.