Abstract
Hydration structures surrounding protein molecules have great influences on folding, stability, physical properties and functions of the molecules. In spite of this fact, X-ray protein crystallography have not sufficiently contributed on hydration structure analyses of proteins. Recent progress in cryogenic techniques enables us to analyze hydration structures of proteins. Cryogenic analyses have provided the structural information on hydration patterns around hydrophobic residues and network structures formed by hydration water molecules. New insights into the hydration structures of proteins have been given by cryogenic X-ray crystallography.
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