Purification, crystallization and preliminary X-ray diffraction studies of the archaeal virus resolvase SIRV2
- European Molecular Biology Laboratory (EMBL), Meyerhofstrasse 1, D-69117 Heidelberg (Germany)
- MPI für Züchtungsforschung, Carl-von-Linné-Weg 10, 50829 Köln (Germany)
The Holliday junction resolvase of the archaeal virus SIRV2 infecting the archaeon Sulfolobus islandicus has been crystallized and a full data set has been collected at 3.4 Å resolution. Analysis of the self-rotation function suggests the presence of two dimers in the asymmetric unit with a solvent content of 77%. The Holliday junction (or four-way junction) is the universal DNA intermediate whose interaction with resolving proteins is one of the major events in the recombinational process. These proteins, called DNA junction-resolving enzymes or resolvases, bind to the junction and catalyse DNA cleavage, promoting the release of two DNA duplexes. SIRV2 Hjc, a viral resolvase infecting a thermophylic archaeon, has been cloned, expressed and purified. Crystals have been obtained in space group C2, with unit-cell parameters a = 147.8, b = 99.9, c = 87.6, β = 109.46°, and a full data set has been collected at 3.4 Å resolution. The self-rotation function indicates the presence of two dimers in the asymmetric unit and a high solvent content (77%). Molecular-replacement trials using known similar resolvase structures have so far been unsuccessful, indicating possible significant structural rearrangements.
- OSTI ID:
- 22356009
- Journal Information:
- Acta Crystallographica. Section F, Vol. 61, Issue Pt 5; Other Information: PMCID: PMC1952314; PMID: 16511081; PUBLISHER-ID: fw5032; OAI: oai:pubmedcentral.nih.gov:1952314; Copyright (c) International Union of Crystallography 2005; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
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