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

doi:10.1107/S1744309107022762

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

School of Medicine

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3 Scopus citations

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 language	English (US)
Pages (from-to)	542-545
Number of pages	4
Journal	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Volume	63
Issue number	6
DOIs	https://doi.org/10.1107/S1744309107022762
State	Published - 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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10.1107/S1744309107022762

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Crystallization and preliminary crystallographic characterization of the origin-binding domain of the bacteriophage λ O replication initiator. / Struble, E. B.; Gittis, A. G.; Bianchet, M. A. et al.
In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 63, No. 6, 05.05.2007, p. 542-545.

Research output: Contribution to journal › Article › peer-review

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AU - Struble, E. B.

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AU - McMacken, R.

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AB - 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.

KW - Bacteriophage λ

KW - O replication initiator

KW - Origin-binding domain

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

Abstract

Keywords

ASJC Scopus subject areas

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