首页> 美国卫生研究院文献>Acta Crystallographica Section F: Structural Biology and Crystallization Communications >Expression purification crystallization and preliminary X-ray diffraction analysis of the soluble domain of PPA0092 a putative nitrite reductase from Propionibacterium acnes
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Expression purification crystallization and preliminary X-ray diffraction analysis of the soluble domain of PPA0092 a putative nitrite reductase from Propionibacterium acnes

机译:PPA0092可溶性结构域的表达纯化结晶和初步X射线衍射分析该结构域是痤疮丙酸杆菌的一种假定的亚硝酸盐还原酶

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摘要

The soluble domain (residues 483–913) of PPA0092, a putative copper-containing nitrite reductase from Propionibacterium acnes KPA171202, has been overexpressed in Escherichia coli. The purified recombinant protein was crystallized using the hanging-drop vapour-diffusion method. X-ray diffraction data were collected and processed to a maximum resolution of 2.4 Å. The crystal belonged to space group P213, with unit-cell parameters a = b = c = 108.63 Å. Preliminary diffraction data show that one molecule is present in the asymmetric unit; this corresponds to a V M of 2.1 Å3 Da−1.
机译:PPA0092的可溶域(483-913残基)是痤疮丙酸杆菌KPA171202的一种推定的含铜亚硝酸盐还原酶,已在大肠杆菌中过表达。使用悬滴蒸汽扩散法将纯化的重组蛋白结晶。收集X射线衍射数据并处理为最大分辨率为2.4Å。该晶体属于空间群P213,单位晶胞参数a = b = c = 108.63Å。初步衍射数据表明,不对称单元中存在一个分子。这对应于V M为2.1sÅ 3 Da -1

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