Journal
PHYSICAL REVIEW LETTERS
Volume 95, Issue 21, Pages -Publisher
AMERICAN PHYSICAL SOC
DOI: 10.1103/PhysRevLett.95.218103
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The dynamical origin of the x-ray diffuse scattering by crystals of a protein, Staphylococcal nuclease, is determined using molecular dynamics simulation. A smooth, nearly isotropic scattering shell at q=0.28 angstrom(-1) originates from equal contributions from correlations in nearest-neighbor water molecule dynamics and from internal protein motions, the latter consisting of alpha-helix pitch and inter-beta-strand fluctuations. Superposed on the shell are intense, three-dimensional scattering features that originate from a very small number of slowly varying (> 10 ns) collective motions. The individual three-dimensional features are assigned to specific collective motions in the protein, and some of these explicitly involve potentially functional active-site deformations.
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