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Publication Abstract from PubMed

Advances in structural biology have relied heavily on synchrotron cryo-crystallography and cryogenic electron microscopy to elucidate biological processes and for drug discovery. However, disparities between cryogenic and room-temperature (RT) crystal structures pose challenges. Here, Cryo2RT, a high-throughput RT data-collection method from cryo-cooled crystals that leverages the cryo-crystallography workflow, is introduced. Tested on endothiapepsin crystals with four soaked fragments, thaumatin and SARS-CoV-2 3CL(pro), Cryo2RT reveals unique ligand-binding poses, offers a comparable throughput to cryo-crystallography and eases the exploration of structural dynamics at various temperatures.

Cryo2RT: a high-throughput method for room-temperature macromolecular crystallography from cryo-cooled crystals.,Huang CY, Aumonier S, Olieric V, Wang M Acta Crystallogr D Struct Biol. 2024 Aug 1;80(Pt 8):620-628. doi: , 10.1107/S2059798324006697. Epub 2024 Jul 25. PMID:39052318^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.