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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | 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 |
| Description | Country affiliation: Taiwan Author Affiliation: Chen CD ( Department of Physics, National Tsing-Hua University, Hsinchu 30013, Taiwan.) |
| Abstract | 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%. |
| File Format | HTM / HTML |
| ISSN | 2053230X |
| e-ISSN | 17443091 |
| Journal | Acta Crystallographica Section F Structural Biology and Crystallization Communications |
| Issue Number | Pt 6 |
| Volume Number | 63 |
| Language | English |
| Publisher | Wiley |
| Publisher Date | 2007-06-01 |
| Publisher Place | Great Britain (UK) |
| Access Restriction | Open |
| Subject Keyword | Discipline Crystallography Discipline Biophysics Discipline Molecular Biology Discipline Biochemistry Bacterial Proteins Isolation & Purification Deinococcus Enzymology Transaminases Chemistry Crystallization Crystallography, X-ray Isoleucine Leucine Valine Research Support, Non-u.s. Gov't |
| Content Type | Text |
| Resource Type | Article |
| Subject | Genetics Structural Biology Medicine Biochemistry Biophysics Condensed Matter Physics |
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