Open Access
Preliminary X‐ray crystallographic analysis of sulfide:quinone oxidoreductase from Acidithiobacillus ferrooxidans
Acta Crystallographica Section FPeer ReviewedZhang Yanfei +52009Journals
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 P 4 2 2 1 2, with unit‐cell parameters a = b = 131.7, c = 208.8 Å, and diffracted to 2.3 Å 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 Å 3  Da −1 and a solvent content of 72.9%.

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