Open AccessPurification, crystallization and preliminary X‐ray diffraction analysis of a cystathionine β‐synthase domain‐containing protein, CDCP2, from Arabidopsis thaliana
Author(s) -
Jeong ByungCheon,
Yoo Kyoung Shin,
Jung Kwang Wook,
Shin Jeong Sheop,
Song Hyun Kyu
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108025128
Subject(s) - polyethylene glycol , crystallography , arabidopsis thaliana , crystallization , peg ratio , x ray crystallography , recombinant dna , chemistry , protein crystallization , resolution (logic) , diffraction , molecule , solvent , atp synthase , biochemistry , enzyme , gene , mutant , optics , physics , organic chemistry , artificial intelligence , computer science , finance , economics
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 P 3 1 21 or P 3 2 21, 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%.