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

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

Research output: Contribution to journalArticle

4 Citations (Scopus)

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 P3 121 or P3 221, 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%.

Original languageEnglish
Pages (from-to)825-827
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume64
Issue number9
DOIs
Publication statusPublished - 2008 Sep 11

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Structural Biology
  • Genetics
  • Condensed Matter Physics

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