Preliminary X-ray crystallographic analysis of sulfide:quinone oxidoreductase from Acidithiobacillus ferrooxidans.
The gene product of open reading frame AFE_1293 from Acidithiobacillus ferrooxidans ATCC 23270 is annotated as encoding a sulfide:quinone oxidoreductase, an enzyme that catalyses electron transfer from sulfide to quinone. Following overexpression in Escherichia coli, the enzyme was purified and crystallized using the hanging-drop vapour-diffusion method. The native crystals belonged to the tetragonal space group P4(2)2(1)2, with unit-cell parameters a = b = 131.7, c = 208.8 A, and diffracted to 2.3 A resolution. Preliminary crystallographic analysis indicated the presence of a dimer in the asymmetric unit, with an extreme value of the Matthews coefficient (V(M)) of 4.53 A(3) Da(-1) and a solvent content of 72.9%.
Zhang
Yanfei
Y
Group in Protein Structure and Function, Department of Biochemistry, University of Alberta, Edmonton, Alberta T6G 2H7, Canada.
Cherney
Maia M
MM
Solomonson
Matthew
M
Liu
Jianshe
J
James
Michael N G
MN
Weiner
Joel H
JH
D000595:Amino Acid Sequence; D003001:Cloning, Molecular; D018360:Crystallography, X-Ray; D008969:Molecular Sequence Data; D011487:Protein Conformation; D011808:Quinone Reductases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification; D017386:Sequence Homology, Amino Acid; D013855:Thiobacillus / Q000201:enzymology*
D011994:Recombinant Proteins; D011808:Quinone Reductases; C073412:sulfide quinone reductase