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Despite images that suggest proteins are rigid in crystals, they can and do, undergo substantial variations in structure. Both characterizations of the ensemble and observations of time-dependent structural changes are possible in crystals. The results are generally consistent with spectroscopic and other measurements, which is not surprising given that the water content of crystals is about the same as that in living cells. Furthermore, simple models of proteins as elastic networks work surprisingly well in describing protein motions in crystals. Apparently the free energies of crystallization of proteins are not large compared to the fluctuations that occur at physiological temperature. New examples will be given which support these variously accepted claims. Host: Mike Wall, CCS-3 |