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Updated: Jul 14, 2026

Iterative Optimization of DNA Duplexes for Crystallization of SeqA-DNA Complexes
Published on: November 1, 2012
Crystallization and preliminary crystallographic characterization of the origin-binding domain of the bacteriophage
E B Struble1, A G Gittis, M A Bianchet
1Department of Biophysics, Johns Hopkins University, Baltimore, MD 21218, USA. evi.struble@nist.gov
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.
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