title: Crystallization and preliminary crystallographic characterization of the origin-binding domain of the bacteriophage lambda O replication initiator.
abstract: The bacteriophage lambda O protein binds to the lambda replication origin (orilambda) and serves as the primary replication initiator for the viral genome. The binding energy derived from the binding of O to orilambda 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 lambda O that diffract to 2.5 A is reported. Anomalous dispersion methods will be used to solve this structure.
authors.affiliation: Department of Biophysics, Johns Hopkins University, Baltimore, MD 21218, USA. evi.struble@nist.gov
authors.forename: E B
authors.initials: EB
authors.lastname: Struble
authors.forename: A G
authors.initials: AG
authors.lastname: Gittis
authors.forename: M A
authors.initials: MA
authors.lastname: Bianchet
authors.forename: R
authors.initials: R
authors.lastname: McMacken
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D004268:DNA-Binding Proteins / Q000737:chemistry*; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D014764:Viral Proteins / Q000737:chemistry*
chemical_list: D004268:DNA-Binding Proteins; C027812:O protein, Bacteriophage lambda; D014764:Viral Proteins; C055789:origin-binding proteins, viral