Structure of the amino-terminal domain of phage 434 represser at 2.0 Å resolution

A. Mondragón*, S. Subbiah, S. C. Almo, M. Drottar, S. C. Harrison

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

127 Scopus citations

Abstract

The crystal structure of the amino-terminal domain of phage 434 represser has been solved using molecular replacement methods and refined to an R-factor of 19.3% against data to 2.0 Å resolution. The protein comprises five short α-helices. Two of these form a helix-turn-helix motif, very similar to those found in related proteins. The protein is remarkably similar to the Cro protein from the same phage.

Original languageEnglish (US)
Pages (from-to)189-200
Number of pages12
JournalJournal of Molecular Biology
Volume205
Issue number1
DOIs
StatePublished - Jan 5 1989

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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