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

ABSTRACT: Cystathione beta-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 A resolution using synchrotron radiation and belonged to the trigonal space group P3(1)21 or P3(2)21, with unit-cell parameters a = b = 56.360, c = 82.596 A, alpha = beta = 90, gamma = 120 degrees . The asymmetric unit contains one CDCP2 molecule and the solvent content is approximately 41%.

SUBMITTER: Jeong BC

PROVIDER: S-EPMC2531278 | biostudies-literature | 2008 Sep

REPOSITORIES: biostudies-literature

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

Jeong Byung Cheon BC Yoo Kyoung Shin KS Jung Kwang Wook KW Shin Jeong Sheop JS Song Hyun Kyu HK

Acta crystallographica. Section F, Structural biology and crystallization communications 20080820 Pt 9

Cystathione beta-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 A resolution using synchrotron radiation and belonged to the trigonal space group P3(1)21 or P3(2)21, with unit-cell parameters a = b = 56.360, c = 82.59 ...[more]

PMID: 18765915

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