多杀巴斯德氏菌毒素催化结构域的结晶及初步晶体学研究
Crystallization and preliminary crystallographic studies of the Pasteurella multocida toxin catalytic domain.
作者信息
Miyazawa Masayuki, Kitadokoro Kengo, Kamitani Shigeki, Shime Hiroaki, Horiguchi Yasuhiko
机构信息
Research Institute for Microbial Diseases, Osaka University, 3-1 Yamada-oka, Suita-shi, Osaka 565-0871, Japan.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Sep 1;62(Pt 9):906-8. doi: 10.1107/S1744309106030375. Epub 2006 Aug 18.
Abstract
The C-terminal catalytic domain of Pasteurella multocida toxin, which is the virulence factor of the organism in P. multocida, has been expressed, purified and subsequently crystallized using the sitting-drop vapour-diffusion technique. Native diffraction data to 1.9 A resolution were obtained at the BL44XU beamline of SPring-8 from a flash-frozen crystal at 100 K. The crystals belong to space group C2, with unit-cell parameters a = 111.0, b = 150.4, c = 77.1 A, beta = 105.5 degrees, and are likely to contain one C-PMT (726 residues) per asymmetric unit.
摘要
多杀巴斯德氏菌毒素的C端催化结构域是该生物体的毒力因子，已通过坐滴气相扩散技术进行表达、纯化并随后结晶。在SPring-8的BL44XU光束线上，从100 K下快速冷冻的晶体获得了分辨率为1.9 Å的原生衍射数据。晶体属于空间群C2，晶胞参数为a = 111.0、b = 150.4、c = 77.1 Å、β = 105.5°，每个不对称单元可能包含一个C-PMT（726个残基）。
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