Crystallographic Refinement
Iterative adjustment of atomic coordinates, B-factors, and occupancies to maximise agreement with the observed amplitudes while restrained to known bond lengths, angles, and planarity. Because data-to-parameter ratios are poor at typical protein resolutions, geometric restraints and the choice of B-factor model carry much of the information.
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Iterative adjustment of atomic coordinates, B-factors, and occupancies to maximise agreement with the observed amplitudes while restrained to known bond lengths, angles, and planarity. Because data-to-parameter ratios are poor at typical protein resolutions, geometric restraints and the choice of B-factor model carry much of the information.
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