Instrumentation and experimental procedures for robust collection of X-ray diffraction data from protein crystals across physiological temperatures.

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. T

SUBMITTER: Doukov T 

PROVIDER: S-EPMC7710493 | biostudies-literature | 2020 Dec

REPOSITORIES: biostudies-literature