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Crystallization and preliminary X‐ray analysis of a RecB‐family nuclease from the archaeon Pyrococcus abyssi

Crystallization and preliminary X‐ray analysis of a RecB‐family nuclease from the archaeon... Nucleases are required to process and repair DNA damage in living cells. One of the best studied nucleases is the RecB protein, which functions in Escherichia coli as a component of the RecBCD enzyme complex that amends double‐strand breaks in DNA. Although archaea do not contain the RecBCD complex, a RecB‐like nuclease from Pyrococcus abyssi has been cloned, expressed and purified. The protein was crystallized by the sitting‐drop vapour‐diffusion method using polyethylene glycol 8000 as the precipitant. The crystals belong to the orthorhombic space group C2221, with unit‐cell parameters a = 81.5, b = 159.8, c = 100.8 Å. Self‐rotation function and native Patterson map calculations revealed that there is a dimer in the asymmetric unit with its local twofold axis running parallel to the crystallographic twofold screw axis. The crystals diffracted to about 2 Å and a complete native data set was collected to 2.65 Å resolution. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Acta Crystallographica Section F Wiley

Crystallization and preliminary X‐ray analysis of a RecB‐family nuclease from the archaeon Pyrococcus abyssi

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References (8)

Publisher
Wiley
Copyright
Copyright © 2007 Wiley Subscription Services, Inc., A Wiley Company
ISSN
1744-3091
eISSN
1744-3091
DOI
10.1107/S1744309107015278
pmid
17565182
Publisher site
See Article on Publisher Site

Abstract

Nucleases are required to process and repair DNA damage in living cells. One of the best studied nucleases is the RecB protein, which functions in Escherichia coli as a component of the RecBCD enzyme complex that amends double‐strand breaks in DNA. Although archaea do not contain the RecBCD complex, a RecB‐like nuclease from Pyrococcus abyssi has been cloned, expressed and purified. The protein was crystallized by the sitting‐drop vapour‐diffusion method using polyethylene glycol 8000 as the precipitant. The crystals belong to the orthorhombic space group C2221, with unit‐cell parameters a = 81.5, b = 159.8, c = 100.8 Å. Self‐rotation function and native Patterson map calculations revealed that there is a dimer in the asymmetric unit with its local twofold axis running parallel to the crystallographic twofold screw axis. The crystals diffracted to about 2 Å and a complete native data set was collected to 2.65 Å resolution.

Journal

Acta Crystallographica Section F – Wiley

Published: May 1, 2007

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