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:
影响因子:
--
通讯作者:
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
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%.