Chen Chung-Der, Huang Tien-Feng, Lin Chih-Hao, Guan Hong-Hsiang, Hsieh Yin-Cheng, Lin Yi-Hung, Huang Yen-Chieh, Liu Ming-Yih, Chang Wen-Chang, Chen Chun-Jung
Department of Physics, National Tsing-Hua University, Hsinchu 30013, Taiwan.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Jun 1;63(Pt 6):492-4. doi: 10.1107/S1744309107020842. Epub 2007 May 5.
The branched-chain amino-acid aminotransferase (BCAT), which requires pyridoxal 5'-phosphate (PLP) as a cofactor, is a key enzyme in the biosynthetic pathway of the hydrophobic amino acids leucine, isoleucine and valine. DrBCAT from Deinococcus radiodurans, which has a molecular weight of 40.9 kDa, was crystallized using the hanging-drop vapour-diffusion method. According to X-ray diffraction data to 2.50 A resolution from a DrBCAT crystal, the crystal belongs to space group P2(1)2(1)2(1), with unit-cell parameters a = 56.37, b = 90.70, c = 155.47 A. Preliminary analysis indicates the presence of two DrBCAT molecules in the asymmetric unit, with a solvent content of 47.52%.
支链氨基酸转氨酶（BCAT）以磷酸吡哆醛（PLP）作为辅因子，是疏水性氨基酸亮氨酸、异亮氨酸和缬氨酸生物合成途径中的关键酶。来自耐辐射球菌的DrBCAT分子量为40.9 kDa，采用悬滴气相扩散法进行结晶。根据DrBCAT晶体2.50 Å分辨率的X射线衍射数据，该晶体属于空间群P2(1)2(1)2(1)，晶胞参数a = 56.37，b = 90.70，c = 155.47 Å。初步分析表明，不对称单元中存在两个DrBCAT分子，溶剂含量为47.52%。
