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Preliminary X-ray crystallographic analysis of sulfide:quinone oxidoreductase from Acidithiobacillus ferrooxidans

机译:铁酸酸性硫杆菌的硫化物:醌氧化还原酶的初步X射线晶体学分析

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摘要

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 P42212, 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 Å3 Da−1 and a solvent content of 72.9%.
机译:来自铁氧化酸硫硫杆菌ATCC 23270的开放阅读框AFE_1293的基因产物被注释为编码硫化物:醌氧化还原酶,该酶催化电子从硫化物转移到醌。在大肠杆菌中过量表达后,使用悬滴蒸汽扩散法纯化和结晶该酶。原始晶体属于四边形空间群P42212,单位晶胞参数a = b = 131.7,c = 208.8,并衍射至2.3分辨率。初步晶体学分析表明不对称单元中存在二聚体,其马修斯系数(VM)的极值为4.53Å 3 Da -1 占72.9%。

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