Yang Jin Kuk, Chang Changsoo, Cho Seung-Je, Lee Jae Young, Yu Yeon Gyu, Eom Soo Hyun, Suh Se Won
Structural Proteomics Laboratory, School of Chemistry and Molecular Engineering, College of Natural Sciences, Seoul National University, Seoul 151-742, South Korea.
Acta Crystallogr D Biol Crystallogr. 2003 Mar;59(Pt 3):563-5. doi: 10.1107/s0907444903000076. Epub 2003 Feb 21.
A putative aspartate aminotransferase from the hyperthermophilic archaeon Methanococcus jannaschii encoded by the Mj0684 gene has been overexpressed in Escherichia coli and crystallized at 296 K using the sitting-drop vapour-diffusion method. The crystals belong to space group P4(1)2(1)2 (or P4(3)2(1)2), with unit-cell parameters a = b = 111.87, c = 60.86 A. They diffract to 2.2 A resolution using Cu Kalpha X-rays. The asymmetric unit contains a single subunit of the recombinant Mj0684 gene product, giving a corresponding V(M) of 2.25 A(3) Da(-1) and a solvent content of 45.3% by Volume. An X-ray diffraction data set has been collected to 2.2 A at 295 K.
由Mj0684基因编码的来自嗜热古菌詹氏甲烷球菌的一种假定天冬氨酸转氨酶已在大肠杆菌中过表达,并采用坐滴气相扩散法于296 K下结晶。晶体属于空间群P4(1)2(1)2(或P4(3)2(1)2),晶胞参数a = b = 111.87,c = 60.86 Å。使用Cu Kα X射线,它们的衍射分辨率达到2.2 Å。不对称单元包含重组Mj0684基因产物的一个亚基,相应的V(M)为2.25 ų Da⁻¹,溶剂含量为45.3%(体积)。已在295 K下收集了分辨率为2.2 Å的X射线衍射数据集。