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 |
|---|---|
| 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 - 五月 5 2007 |
| 對外發佈 | Yes |
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Genetics
- Condensed Matter Physics
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引用此
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