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Purification, crystallization and preliminary X‐ray diffraction analysis of a cystathionine β‐synthase domain‐containing protein, CDCP2, from Arabidopsis thaliana

Purification, crystallization and preliminary X‐ray diffraction analysis of a cystathionine... Cystathione β‐synthase domain‐containing protein 2 (CDCP2) from Arabidopsis thaliana has been overexpressed and purified to homogeneity. As an initial step towards three‐dimensional structure determination, crystals of recombinant CDCP2 protein have been obtained using polyethylene glycol 8000 as a precipitant. The crystals diffracted to 2.4 Å resolution using synchrotron radiation and belonged to the trigonal space group P3121 or P3221, with unit‐cell parameters a = b = 56.360, c = 82.596 Å, α = β = 90, γ = 120°. The asymmetric unit contains one CDCP2 molecule and the solvent content is approximately 41%. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Acta Crystallographica Section F Wiley

Purification, crystallization and preliminary X‐ray diffraction analysis of a cystathionine β‐synthase domain‐containing protein, CDCP2, from Arabidopsis thaliana

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References (11)

Publisher
Wiley
Copyright
International Union of Crystallography, 2008
ISSN
1744-3091
eISSN
1744-3091
DOI
10.1107/S1744309108025128
pmid
18765915
Publisher site
See Article on Publisher Site

Abstract

Cystathione β‐synthase domain‐containing protein 2 (CDCP2) from Arabidopsis thaliana has been overexpressed and purified to homogeneity. As an initial step towards three‐dimensional structure determination, crystals of recombinant CDCP2 protein have been obtained using polyethylene glycol 8000 as a precipitant. The crystals diffracted to 2.4 Å resolution using synchrotron radiation and belonged to the trigonal space group P3121 or P3221, with unit‐cell parameters a = b = 56.360, c = 82.596 Å, α = β = 90, γ = 120°. The asymmetric unit contains one CDCP2 molecule and the solvent content is approximately 41%.

Journal

Acta Crystallographica Section FWiley

Published: Sep 1, 2008

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