摘要
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%.
原文 | 英語 |
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頁(從 - 到) | 492-494 |
頁數 | 3 |
期刊 | Acta Crystallographica Section F: Structural Biology and Crystallization Communications |
卷 | 63 |
發行號 | 6 |
DOIs | |
出版狀態 | 已發佈 - 5月 5 2007 |
對外發佈 | 是 |
ASJC Scopus subject areas
- 生物物理學
- 結構生物學
- 生物化學
- 遺傳學
- 凝聚態物理學