Crystallization and preliminary crystallographic characterization of the origin-binding domain of the bacteriophage λ O replication initiator

E. B. Struble, A. G. Gittis, M. A. Bianchet, R. McMacken

Research output: Contribution to journalArticle

Abstract

The bacteriophage λ O protein binds to the λ replication origin (oriλ) and serves as the primary replication initiator for the viral genome. The binding energy derived from the binding of O to oriλ is thought to help drive DNA opening to facilitate initiation of DNA replication. Detailed understanding of this process is severely limited by the lack of high-resolution structures of O protein or of any lambdoid phage-encoded paralogs either with or without DNA. The production of crystals of the origin-binding domain of λ O that diffract to 2.5 Å is reported. Anomalous dispersion methods will be used to solve this structure.

Original languageEnglish (US)
Pages (from-to)542-545
Number of pages4
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume63
Issue number6
DOIs
StatePublished - May 5 2007

Keywords

  • Bacteriophage λ
  • O replication initiator
  • Origin-binding domain

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics

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