Crystallization and preliminary crystallographic characterization of the origin-binding domain of the bacteriophage lambda O replication initiator.
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.
Struble
E B
EB
Department of Biophysics, Johns Hopkins University, Baltimore, MD 21218, USA. evi.struble@nist.gov
Gittis
A G
AG
Bianchet
M A
MA
McMacken
R
R
D003460:Crystallization; D018360:Crystallography, X-Ray; D004268:DNA-Binding Proteins / Q000737:chemistry*; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D014764:Viral Proteins / Q000737:chemistry*
D004268:DNA-Binding Proteins; C027812:O protein, Bacteriophage lambda; D014764:Viral Proteins; C055789:origin-binding proteins, viral