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- W4313458413 endingPage "94" @default.
- W4313458413 startingPage "78" @default.
- W4313458413 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 advantages and physical principles of, and methods for, crystallographic data collection at noncryogenic temperatures and some factors relevant to interpreting the resulting data are discussed. For room-temperature data collection to realize its potential within the structural biology toolkit, streamlined and standardized methods for delivering crystals prepared in the home laboratory to the synchrotron and for automated handling and data collection, similar to those for cryocrystallography, should be implemented." @default.
- W4313458413 created "2023-01-06" @default.
- W4313458413 creator A5061474199 @default.
- W4313458413 date "2023-01-01" @default.
- W4313458413 modified "2023-10-16" @default.
- W4313458413 title "Determining biomolecular structures near room temperature using X-ray crystallography: concepts, methods and future optimization" @default.
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