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Experimental Techniques for Collecting X-Ray Diffraction Data from Protein Crystals over a Broad Temperature Range

Swapna Sanika

Traditional Xâ?ray diffraction facts collected at cryoâ?temperatures have introduced profitable insights into the threeâ?dimensional structures of proteins, imparting the backbone of shape–function studies. While cryoâ?cooling mitigates radiation harm, cryoâ? temperatures can regulate protein conformational ensembles and solvent shape. Furthermore, conformational ensembles underlie protein function and energetics, and present day advances in roomâ?temperature Xâ?ray crystallography have introduced conformational heterogeneity statistics that can be right away related to natural function.