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 journalArticle

110 Scopus citations

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 (US)
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
StatePublished - Mar 15 1994

Keywords

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

ASJC Scopus subject areas

  • General

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    Skinner, M. M., Zhang, H., Leschnitzer, D. H., Guan, Y., Bellamy, H., Sweet, R. M., Gray, C. W., Konings, R. N. H., Wang, A. H. J., & Terwilliger, T. C. (1994). Structure of the gene V protein of bacteriophage f1 determined by multiwavelength x-ray diffraction on the selenomethionyl protein. Proceedings of the National Academy of Sciences of the United States of America, 91(6), 2071-2075. https://doi.org/10.1073/pnas.91.6.2071