Purification, crystallization and preliminary X-ray diffraction studies of the archaeal virus resolvase SIRV2

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
Eric EnnifarDietrich Suck

Abstract

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, beta = 109.46 degrees, and a full data set has been collected at 3.4 A 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.

References

May 2, 2001·Proceedings of the National Academy of Sciences of the United States of America·C S BondW N Hunter
Jun 5, 2001·Nature Reviews. Molecular Cell Biology·D M Lilley, M F White
Jun 12, 2001·Journal of Molecular Biology·R P BirkenbihlB Kemper
Dec 25, 2002·Acta Crystallographica. Section D, Biological Crystallography·Claire L MiddletonCharles S Bond
Oct 14, 2004·Nucleic Acids Research·Claire L MiddletonCharles S Bond

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Citations

Mar 3, 2006·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Christian BiertümpfelClaude Sauter
Mar 3, 2006·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·N UmadeviN Narayana

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