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Crystallization and preliminary X-ray study of Pk-REC from a hyperthermophilic archaeon, Pyrococcus kodakaraensis KOD1

Crystallization and preliminary X-ray study of Pk-REC from a hyperthermophilic archaeon,... Pk-REC is a protein which binds to DNA and catalyzes the central step of recombination and repair. The protein was crystallized using the hanging-drop vapour-diffusion method with PEG as a precipitant. Two orthorhombic crystal forms I and II with the same space group P212121 were obtained at pH 8.0 using PEG 3000 and PEG 550 monomethylether, respectively. The unit-cell parameters were a = 151, b = 174, c = 241 A for form I and a = 151, b = 176, c = 300 A for form II, indicating that the asymmetric unit contains more than 20 molecules. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Acta Crystallographica Section D: Biological Crystallography International Union of Crystallography

Crystallization and preliminary X-ray study of Pk-REC from a hyperthermophilic archaeon, Pyrococcus kodakaraensis KOD1

Crystallization and preliminary X-ray study of Pk-REC from a hyperthermophilic archaeon, Pyrococcus kodakaraensis KOD1


Abstract

Pk-REC is a protein which binds to DNA and catalyzes the central step of recombination and repair. The protein was crystallized using the hanging-drop vapour-diffusion method with PEG as a precipitant. Two orthorhombic crystal forms I and II with the same space group P212121 were obtained at pH 8.0 using PEG 3000 and PEG 550 monomethylether, respectively. The unit-cell parameters were a = 151, b = 174, c = 241 A for form I and a = 151, b = 176, c = 300 A for form II, indicating that the asymmetric unit contains more than 20 molecules.

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References (6)

Publisher
International Union of Crystallography
Copyright
Copyright (c) 2000 International Union of Crystallography
Subject
binding proteins, Pk-REC
ISSN
0907-4449
eISSN
1399-0047
DOI
10.1107/S0907444900002821
Publisher site
See Article on Publisher Site

Abstract

Pk-REC is a protein which binds to DNA and catalyzes the central step of recombination and repair. The protein was crystallized using the hanging-drop vapour-diffusion method with PEG as a precipitant. Two orthorhombic crystal forms I and II with the same space group P212121 were obtained at pH 8.0 using PEG 3000 and PEG 550 monomethylether, respectively. The unit-cell parameters were a = 151, b = 174, c = 241 A for form I and a = 151, b = 176, c = 300 A for form II, indicating that the asymmetric unit contains more than 20 molecules.

Journal

Acta Crystallographica Section D: Biological CrystallographyInternational Union of Crystallography

Published: May 1, 2000

Keywords: binding proteins; Pk -REC.

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