Akita Masatake, Hatada Yuji, Hidaka Yuko, Ohta Yukari, Takada Masayasu, Nakagawa Yoshinori, Ogawa Koichi, Nakakuki Teruo, Ito Susumu, Horikoshi Koki
Japan Marine Science and Technology Center, 2-15 Natsushima, Yokosuka 237-0061, Japan.
Acta Crystallogr D Biol Crystallogr. 2004 Mar;60(Pt 3):586-7. doi: 10.1107/S0907444904001076. Epub 2004 Feb 25.
A gamma-cyclodextrin glycosyltransferase (EC 2.4.1.19) from Bacillus clarkii was crystallized using the hanging-drop vapour-diffusion method at 293 K. X-ray diffraction data were collected to 2.2 A. The crystal belongs to space group R3, with unit-cell parameters a = b = 211.6, c = 52.7 A. The asymmetric unit contains one protein molecule, with a corresponding V(M) of 3.03 A(3) Da(-1) and a solvent content of 59.4%. Molecular replacement was successfully carried out using a homology model based on the three-dimensional structure of the CGTase from Thermonanaerobacterium thermosulfurigenes EM1 as a search model.
利用悬滴气相扩散法在293 K下对来自克拉克芽孢杆菌的γ-环糊精糖基转移酶(EC 2.4.1.19)进行了结晶。收集到了分辨率为2.2 Å的X射线衍射数据。晶体属于R3空间群,晶胞参数a = b = 211.6,c = 52.7 Å。不对称单元包含一个蛋白质分子,其对应的V(M)为3.03 ų Da⁻¹,溶剂含量为59.4%。以嗜热栖热硫化叶菌EM1的CGTase三维结构为搜索模型,基于同源性模型成功进行了分子置换。