Purification, crystallization and preliminary X-ray diffraction analysis of a cystathionine beta-synthase domain-containing protein, CDCP2, from Arabidopsis thaliana
- Authors
- Jeong, Byung-Cheon; Yoo, Kyoung Shin; Jung, Kwang Wook; Shin, Jeong Sheop; Song, Hyun Kyu
- Issue Date
- 9월-2008
- Publisher
- INT UNION CRYSTALLOGRAPHY
- Keywords
- CDCP2
- Citation
- ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, v.64, pp.825 - 827
- Indexed
- SCIE
SCOPUS
- Journal Title
- ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
- Volume
- 64
- Start Page
- 825
- End Page
- 827
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/122743
- DOI
- 10.1107/S1744309108025128
- ISSN
- 2053-230X
- 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 angstrom 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 angstrom, alpha = beta = 90, gamma = 120 degrees. The asymmetric unit contains one CDCP2 molecule and the solvent content is approximately 41%.
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- Appears in
Collections - College of Life Sciences and Biotechnology > Division of Life Sciences > 1. Journal Articles
- Graduate School > Department of Life Sciences > 1. Journal Articles
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