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

  • Jeong, Byung-Cheon
  • Yoo, Kyoung Shin
  • Jung, Kwang Wook
  • Shin, Jeong Sheop
  • Song, Hyun Kyu
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초록

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%.

키워드

CDCP2CBS DOMAINSAMPCRYSTALSBINDINGCOMPLEXSENSORKINASE
제목
Purification, crystallization and preliminary X-ray diffraction analysis of a cystathionine beta-synthase domain-containing protein, CDCP2, from Arabidopsis thaliana
저자
Jeong, Byung-CheonYoo, Kyoung ShinJung, Kwang WookShin, Jeong SheopSong, Hyun Kyu
DOI
10.1107/S1744309108025128
발행일
2008-09
유형
Article
저널명
Acta Crystallographica Section F: Structural Biology Communications
64
페이지
825 ~ 827