Premium
Combined Rietveld and stereochemical restraint refinement of a protein crystal structure
Author(s) -
Von Dreele R. B.
Publication year - 1999
Publication title -
journal of applied crystallography
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.429
H-Index - 162
ISSN - 1600-5767
DOI - 10.1107/s002188989901064x
Subject(s) - rietveld refinement , crystal structure , crystallography , powder diffraction , chemistry , resolution (logic) , diffraction , metmyoglobin , atom (system on chip) , x ray crystallography , materials science , physics , myoglobin , computer science , optics , organic chemistry , artificial intelligence , embedded system
By combining high‐resolution X‐ray powder diffraction data and stereochemical restraints, Rietveld refinement of protein crystal structures has been shown to be feasible. A refinement of the 1261‐atom protein metmyoglobin was achieved by combining 5338 stereochemical restraints with a 4648‐step ( d min = 3.3 Å) powder diffraction pattern to give the residuals R wp = 2.32%, R p = 1.66%, R ( F 2 ) = 3.10%. The resulting tertiary structure of the protein is essentially identical to that obtained from previous single‐crystal studies.