期刊
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY
卷 72, 期 -, 页码 176-179出版社
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S2059798315022408
关键词
covalent geometry restraints; crystallographic refinement; protein structure; validation; Phenix
资金
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [P01GM063210, R01GM083136] Funding Source: NIH RePORTER
- NIGMS NIH HHS [P01 GM063210, R01 GM083136, R01-GM083136, 1P01 GM063210] Funding Source: Medline
Chemical restraints are a fundamental part of crystallographic protein structure refinement. In response to mounting evidence that conventional restraints have shortcomings, it has previously been documented that using backbone restraints that depend on the protein backbone conformation helps to address these shortcomings and improves the performance of refinements [Moriartyet al. et al. (2014),FEBS J. FEBS J.281 281, 4061-4071]. It is important that these improvements be made available to all in the protein crystallography community. Toward this end, a change in the default geometry library used byPhenix Phenix is described here. Tests are presented showing that this change will not generate increased numbers of outliers during validation, or deposition in the Protein Data Bank, during the transition period in which some validation tools still use the conventional restraint libraries.
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