Crystal structure of DNA recombination protein RuvA and a model for its binding to the Holliday junction

Science

Volumn 274, Issue 5286, 1996, Pages 415-421

  Rafferty, John B ^a   Sedelnikova, Svetlana E ^a   Hargreaves, David ^a   Artymiuk, Peter J ^a   Baker, Patrick J ^a   Sharples, Gary J ^b   Mahdi, Akeel A ^b   Lloyd, Robert G ^b   Rice, David W ^a  

^a UNIVERSITY OF SHEFFIELD   (United Kingdom)

^b UNIVERSITY OF NOTTINGHAM   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

DNA BINDING PROTEIN;

ARTICLE; BACTERIAL GENETICS; CRYSTAL STRUCTURE; DNA BINDING; DNA RECOMBINATION; DNA REPAIR; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; PROTEIN DNA INTERACTION; PROTEIN STRUCTURE;

BACTERIAL PROTEINS; BASE COMPOSITION; CRYSTALLOGRAPHY, X-RAY; DNA HELICASES; DNA, BACTERIAL; DNA-BINDING PROTEINS; ENDODEOXYRIBONUCLEASES; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; HYDROGEN BONDING; MODELS, MOLECULAR; NUCLEIC ACID CONFORMATION; OLIGODEOXYRIBONUCLEOTIDES; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RECOMBINATION, GENETIC;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0029806695     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.274.5286.415     Document Type: Article

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76. We thank M. Legg (Zeneca Agrochemicals, Jealott's Hill, UK) for fermentation of the recombinant cells incorporating selenomethionine; the support staff at the Synchrotron Radiation Source, Daresbury Laboratory, Warrington, UK, for assistance with station alignment; and T. J. Palmer for the program used to analyze the selenomethionine Patterson map. Supported by grants from the UK Biotechnology and Biological Sciences Research Council (BBSRC) and the UK Medical Research Council to P.J.A., R.G.L., and D.W.R., and the Wellcome Trust to P.J.A. and D.W.R. J.B.R. is a BBSRC Technology Foresight Junior Research Fellow. G.J.S. is a Royal Society University Research Fellow. The Krebs Institute is a designated BBSRC Biomolecular Science Centre.