Crystallization and preliminary X-ray analysis of a RecB-family nuclease from the archaeon Pyrococcus abyssi. - Archive ouverte HAL
Article Dans Une Revue Acta crystallographica Section F : Structural biology communications [2014-...] Année : 2007

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

Résumé

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 C222(1), with unit-cell parameters a = 81.5, b = 159.8, c = 100.8 A. 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 A and a complete native data set was collected to 2.65 A resolution.

Dates et versions

hal-00194375 , version 1 (06-12-2007)

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Bin Ren, Joëlle Kuhn, Laurence Meslet-Cladiere, Hannu Myllykallio, Rudolf Ladenstein. Crystallization and preliminary X-ray analysis of a RecB-family nuclease from the archaeon Pyrococcus abyssi.. Acta crystallographica Section F : Structural biology communications [2014-..], 2007, 63 (Pt 5), pp.406-8. ⟨10.1107/S1744309107015278⟩. ⟨hal-00194375⟩
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