Crystallization and preliminary crystallographic studies of Escherichia coli CcmG/DsbE protein.
CcmG/DsbE is a typical thiol/disulfide oxidoreductase, exhibiting a specific reducing activity in a highly oxidizing environment, and is involved in electron transfer during the maturation of c-type cytochromes. Escherichia coli CcmG/DsbE (residues 19-185) has been crystallized using the hanging-drop vapour-diffusion technique. The crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 35.48, b = 48.52, c = 84.78 A. X-ray data have been collected to 1.9 A resolution.
Ouyang
Nan
N
State Key Laboratory of Bio-organic and Natural Products Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai 200032, People's Republic of China.
Chen
Wei-Yan
WY
Li
Qi
Q
Gao
Yong-Guang
YG
Hu
Hong-Yu
HY
Xia
Zong-Xiang
ZX
D003460:Crystallization / Q000379:methods*; D018360:Crystallography, X-Ray; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D011490:Protein Disulfide Reductase (Glutathione) / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification
D029968:Escherichia coli Proteins; C485980:Ccmg protein, E coli; D011490:Protein Disulfide Reductase (Glutathione)