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Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Sep 1;64(Pt 9):825-7. doi: 10.1107/S1744309108025128. Epub 2008 Aug 20.

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

Author information

1
School of Life Sciences and Biotechnology, Korea University, Anam-dong, Seoungbuk-gu, Seoul 136-701, Republic of Korea.

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%.

PMID:
18765915
PMCID:
PMC2531278
DOI:
10.1107/S1744309108025128
[Indexed for MEDLINE]
Free PMC Article

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