Expression, purification, crystallization and preliminary X-ray diffraction analysis of the soluble domain of PPA0092, a putative nitrite reductase from Propionibacterium acnes.
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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DOI：
10.1107/s1744309108040207
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发表时间：
2009-02
期刊：
影响因子：
--
通讯作者：
M. Nojiri;F. Shirota;D. Hira;Shinnichiro Suzuki
中科院分区：
文献类型：
--
作者：
M. Nojiri;F. Shirota;D. Hira;Shinnichiro Suzuki
PPA 0092是一种来自痤疮丙酸杆菌KPA 171202的推定的含铜亚硝酸盐还原酶，其可溶性结构域（残基483-913）已在大肠杆菌中过表达。采用悬滴气相扩散法对纯化的重组蛋白进行结晶。收集X射线衍射数据并处理至最大分辨率2.4 A。晶体属P2（1）3空间群，晶胞参数a = B = c = 108.63 A。初步的衍射数据显示，在不对称单元中存在一个分子;这对应于2.1 A（3）Da（-1）的V（M）。
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 A. The crystal belonged to space group P2(1)3, with unit-cell parameters a = b = c = 108.63 A. Preliminary diffraction data show that one molecule is present in the asymmetric unit; this corresponds to a V(M) of 2.1 A(3) Da(-1).