Structure of the gene V protein of bacteriophage f1 determined by multiwavelength x-ray diffraction on the selenomethionyl protein

Matthew M. Skinner, Hong Zhang, Dale H. Leschnitzer, Yue Guan, Henry Bellamy, Robert M. Sweet, Carla W. Gray, Ruud N.H. Konings, Andrew H.J. Wang, Thomas C. Terwilliger

Research output: Contribution to journalArticlepeer-review

112 Citations (Scopus)

Abstract

The crystal structure of the dimeric gene V protein of bacteriophage f1 was determined using multiwavelength anomalous diffraction on the selenomethionine-containing wild-type and isoleucine-47 → methionine mutant proteins with x-ray diffraction data phased to 2.5 Å resolution. The structure of the wild-type protein has been refined to an R factor of 19.2% using native data to 1.8 Å resolution. The structure of the gene V protein was used to obtain a model for the protein portion of the gene V protein- single-stranded DNA complex.

Original languageEnglish
Pages (from-to)2071-2075
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume91
Issue number6
DOIs
Publication statusPublished - Mar 15 1994
Externally publishedYes

Keywords

  • DNA binding protein
  • protein structure
  • protein-DNA complex
  • synchrotron radiation
  • x-ray crystallography

ASJC Scopus subject areas

  • General

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