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 Å resolution from a DrBCAT crystal, the crystal belongs to space group P21212 1, with unit-cell parameters a = 56.37, b = 90.70, c = 155.47 Å. Preliminary analysis indicates the presence of two DrBCAT molecules in the asymmetric unit, with a solvent content of 47.52%.
|頁（從 - 到）||492-494|
|期刊||Acta Crystallographica Section F: Structural Biology and Crystallization Communications|
|出版狀態||已發佈 - 五月 5 2007|
ASJC Scopus subject areas
- Structural Biology
- Condensed Matter Physics
Chen, C. D., Huang, T. F., Lin, C. H., Guan, H. H., Hsieh, Y. C., Lin, Y. H., Huang, Y. C., Liu, M. Y., Chang, W. C., & Chen, C. J. (2007). Purification, crystallization and preliminary X-ray crystallographic analysis of branched-chain aminotransferase from Deinococcus radiodurans. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 63(6), 492-494. https://doi.org/10.1107/S1744309107020842