The temperature-dependent conformational ensemble of SARS-CoV-2 main protease (M pro ).

Ali Ebrahim Blake T RileyDesigan KumaranBabak Andi Martin R Fuchs Sean M McSweeney Daniel A Keedy

Published in: bioRxiv : the preprint server for biology (2021)

X-ray crystallography at variable temperature for SARS-CoV-2 M pro reveals a complex conformational landscape, including mobile solvent at the catalytic dyad, mercurial conformational heterogeneity in a key substrate-binding loop, and an intramolecular network bridging the active site and dimer interface.

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