Cryo-cooling effect on DHFR crystal studied by replica-exchange molecular dynamics simulations

Cryo-cooling is routinely performed before X-ray diffraction image collection, to reduce the damage to crystal due to ionizing radiations. It has been suggested that, while backbone structures are usually very similar between room-temperature and cryo-temperature, cryo-cooling may hamper biologically relevant dynamics. In this study, crystal of Escherichia coli dihydrofolate reductase (DHFR) is studied with replica-exchange molecular dynamics simulation and results are compared with crystal structure determined at cryo-temperature and room-temperature with time-averaged ensemble method.

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