Montoya G, Svensson C, Savage H, Schwenn J D, Sinning I
European Molecular Biology Laboratory, Structural Biology Programme, 69117 Heidelberg, Germany.
Acta Crystallogr D Biol Crystallogr. 1998 Mar 1;54(Pt 2):281-3. doi: 10.1107/s0907444997010019.
PAPS reductase from E. coli is involved in sulfur metabolism and catalyses the reduction of phospho-adenylyl-sulfate (PAPS) to sulfite. The protein has been cloned, overexpressed and purified from E. coli. Crystallization experiments resulted in crystals suitable for X-ray diffraction. The crystals belong to the orthorhombic space group C2221 with cell dimensions a = 81.9, b = 97.4, c = 109.5 A, and contain one molecule per asymmetric unit. At cryogenic (100 K) temperatures the crystals diffract to a resolution limit of 2.7 A using a rotating anode and to 2.0 A at a synchrotron source.
来自大肠杆菌的PAPS还原酶参与硫代谢，并催化磷酸腺苷硫酸酯（PAPS）还原为亚硫酸盐。该蛋白已从大肠杆菌中克隆、过表达并纯化。结晶实验得到了适合X射线衍射的晶体。这些晶体属于正交空间群C2221，晶胞参数a = 81.9、b = 97.4、c = 109.5 Å，每个不对称单元包含一个分子。在低温（100 K）下，使用旋转阳极时晶体的衍射分辨率极限为2.7 Å，在同步辐射源处为2.0 Å。
