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- W3096624764 abstract "Traditional X-ray diffraction data collected at cryo-temperatures have delivered invaluable insights into the three-dimensional structures of proteins, providing the backbone of structure-function studies. While cryo-cooling mitigates radiation damage, cryo-temperatures can alter protein conformational ensembles and solvent structure. Furthermore, conformational ensembles underlie protein function and energetics, and recent advances in room-temperature X-ray crystallography have delivered conformational heterogeneity information that can be directly related to biological function. Given this capability, the next challenge is to develop a robust and broadly applicable method to collect single-crystal X-ray diffraction data at and above room temperature. This challenge is addressed herein. The approach described provides complete diffraction data sets with total collection times as short as ∼5 s from single protein crystals, dramatically increasing the quantity of data that can be collected within allocated synchrotron beam time. Its applicability was demonstrated by collecting 1.09-1.54 Å resolution data over a temperature range of 293-363 K for proteinase K, thaumatin and lysozyme crystals at BL14-1 at the Stanford Synchrotron Radiation Lightsource. The analyses presented here indicate that the diffraction data are of high quality and do not suffer from excessive dehydration or radiation damage." @default.
- W3096624764 created "2020-11-09" @default.
- W3096624764 creator A5047719348 @default.
- W3096624764 creator A5049482541 @default.
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- W3096624764 date "2020-11-05" @default.
- W3096624764 modified "2023-10-16" @default.
- W3096624764 title "Instrumentation and experimental procedures for robust collection of X-ray diffraction data from protein crystals across physiological temperatures" @default.
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- W3096624764 doi "https://doi.org/10.1107/s1600576720013503" @default.
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