Determining biomolecular structures near room temperature using X-ray crystallography: concepts, methods and future optimization.

ABSTRACT: For roughly two decades, cryocrystallography has been the overwhelmingly dominant method for determining high-resolution biomolecular structures. Competition from single-particle cryo-electron microscopy and micro-electron diffraction, increased interest in functionally relevant information that may be missing or corrupted in structures determined at cryogenic temperature, and interest in time-resolved studies of the biomolecular response to chemical and optical stimuli have driven renewed interest in data collection at room temperature and, more generally, at temperatures from the protein-solvent glass transition near 200 K to ∼350 K. Fischer has recently reviewed practical methods for room-temperature data collection and analysis [Fischer (2021), Q. Rev. Biophys. 54, e1]. Here, the key a

SUBMITTER: Thorne RE 

PROVIDER: S-EPMC9815097 | biostudies-literature | 2023 Jan

REPOSITORIES: biostudies-literature