Conformation-dependent backbone geometry restraints set a new standard for protein crystallographic refinement
Author:
Affiliation:
1. Lawrence Berkeley National Laboratory; Berkeley CA USA
2. Department of Biochemistry and Biophysics; Oregon State University; Corvallis OR USA
3. Department of Bioengineering; University of California Berkeley; Berkeley CA USA
Funder
National Institutes of Health
Publisher
Wiley
Subject
Cell Biology,Molecular Biology,Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/febs.12860/fullpdf
Reference51 articles.
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2. Crystallographic refinement of structure of bovine pancreatic trypsin-inhibitor at 1.5 A resolution;Deisenhofer;Acta Crystallogr B,1975
3. A method for fitting satisfactory models to sets of atomic positions in protein structure refinements;Dodson;Acta Crystallogr A,1976
4. A method of obtaining a stereochemically acceptable protein model which fits a set of atomic coordinates;Ten Eyck;Acta Crystallogr A,1976
5. A restrained-parameter structure-factor least-squares refinement procedure for large asymmetric units;Konnert;Acta Crystallogr A,1976
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