Purification, Crystallization and Preliminary X-ray Analysis of the Dissimilatory Sulfite Reductase from Desulfovibrio vulgaris Miyazaki F

Purification, Crystallization and Preliminary X-ray Analysis of the Dissimilatory Sulfite Reductase from Desulfovibrio vulgaris Miyazaki F
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普通脱硫弧菌 Miyazaki F 异化亚硫酸还原酶的纯化、结晶和初步 X 射线分析

DOI:
10.1107/s1744309110033191
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发表时间:
2010
期刊:
Acta Crystallogr.
影响因子:
--
通讯作者:
Y. Higuchi and W. Lubitz
Y. Higuchi and W. Lubitz
中科院分区:
--
文献类型:
--
作者:
H. Ogata;Y. Shomura;A.G. Agrawal;A.P. Kaur;W. Gartner;Y. Higuchi and W. Lubitz

文献摘要

相似文献

异化亚硫酸盐还原酶(Dsr)在许多硫酸盐还原菌的硫酸盐呼吸过程中起着重要作用。以聚乙二醇(PEG)3350和硫氰酸钾为沉淀剂,采用坐滴气相扩散法在277 K下对脱硫弧菌(Desulfovibrio vulgaris)宫崎F)中的硫酸锶进行了纯化和结晶。使用同步辐射在100 K下从单晶收集到3.7 μ m分辨率的数据集。 Dsr晶体属于空间群P41212,晶胞参数a = B = 163.26,c = 435.32 nm。 根据D. Dsr的三维结构,用分子置换法确定了Dsr的晶体结构。普通的希尔登伯勒。晶体中每个不对称单元含有3个α2β2γ2单元,马修斯系数(VM)为2.35 3 Da−1;溶剂含量估计为47.7%。  
Dissimilatory sulfite reductase (Dsr) plays an important role in sulfate respiration in many sulfate-reducing bacteria. Dsr from Desulfovibrio vulgaris Miyazaki F has been purified and crystallized at 277 K using the sitting-drop vapour-diffusion method with PEG 3350 and potassium thiocyanate as precipitants. A data set was collected to 3.7 Å resolution from a single crystal at 100 K using synchrotron radiation. The Dsr crystal belonged to space group P41212, with unit-cell parameters a = b = 163.26, c = 435.32 Å. The crystal structure of Dsr was determined by the molecular-replacement method based on the three-dimensional structure of Dsr from D. vulgaris Hildenborough. The crystal contained three α2β2γ2 units per asymmetric unit, with a Matthews coefficient (VM) of 2.35 Å3 Da−1; the solvent content was estimated to be 47.7%.