Although X-ray crystallography has traditionally provided a single protein �structure�, it is an ensemble measurement that can reveal alternative conformations, which are hidden at low levels of electrondensity. Modern protein crystallography is based nearly exclusively on X-ray data collected at cryogenic temperatures (~100 K). The cooling process is thought to introduce little bias in the functional interpretation of structural results, because cryogenic temperatures minimally perturb the overall protein backbone fold. However, we have found that cryocooling protein crystals changes conformational distributions, packing quality, and solvation relative to room temperature data. Monitoring room-temperature conformational ensembles by X-ray crystallography can reveal the structural basis formotions crucial for catalysis, ligand binding, and allosteric regulation.

Biophysical dominos: Protein ensembles from room temperature X-ray crystallography

247th National Meeting (2014)

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