Friday, June 12, 2020, 12:00 pm — via Zoom - contact: nsls2user@bnl.gov
X-ray crystallography is a widely utilized technique to provide essential high resolution structural information for proteins and is particularly important to determine inhibitor binding modes for drug development. Modern advances in protein crystallization automation, synchrotron X-ray beamlines and crystallographic software development have enabled the rapid determination of crystal structures which has greatly facilitated drug discovery and development projects. Diffraction data for dozens of protein-inhibitor samples can be collected in a matter of hours and immediately analyzed for inhibitor binding using automated crystallographic software pipelines. As such, information regarding the binding modes of various inhibitors can be quickly obtained which facilitates subsequent optimization. Application of these modern structural biology techniques has been critical to the advancement of ongoing collaborative projects focused on the development of covalent inhibitors that target the 3CL proteases of Norovirus, MERS-CoV, SARS-CoV and SARS-CoV-2.
Hosted by: Ignace Jarrige
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