Purification, crystallization and preliminary X-ray crystallographic analysis of branched-chain aminotransferase from Deinococcus radiodurans.

Chung-Der Chen, Tien-Feng Huang, Chih-Hao Lin, Hong-Hsiang Guan, Yin-Cheng Hsieh, Yi-Hung Lin, Yen-Chieh Huang, Ming-Yih Liu, Wen-Chang Chang, Chun-Jung Chen

Department of Physics, National Tsing-Hua University, Hsinchu 30013, Taiwan.

Acta crystallographica. Section F, Structural biology and crystallization communications 2007 Jun 1

filter terms:

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%.

Citation

Chung-Der Chen, Tien-Feng Huang, Chih-Hao Lin, Hong-Hsiang Guan, Yin-Cheng Hsieh, Yi-Hung Lin, Yen-Chieh Huang, Ming-Yih Liu, Wen-Chang Chang, Chun-Jung Chen. Purification, crystallization and preliminary X-ray crystallographic analysis of branched-chain aminotransferase from Deinococcus radiodurans. Acta crystallographica. Section F, Structural biology and crystallization communications. 2007 Jun 1;63(Pt 6):492-4