Purification, crystallization and preliminary X-ray crystallographic analysis of branched-chain aminotransferase from Deinococcus radiodurans
Abstract
The crystallization of branched-chain aminotransferase from D. radiodurans is described. 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 P2{sub 1}2{sub 1}2{sub 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%.
- Authors:
-
- Department of Physics, National Tsing-Hua University, Hsinchu 30013,Taiwan (China)
- Institute of Biological Chemistry, National Taiwan University, Taipei 110,Taiwan (China)
- Life Science Group, Research Division, National Synchrotron Radiation Research Center, Hsinchu 30076,Taiwan (China)
- Publication Date:
- OSTI Identifier:
- 22360344
- Resource Type:
- Journal Article
- Journal Name:
- Acta Crystallographica. Section F
- Additional Journal Information:
- Journal Volume: 63; Journal Issue: Pt 6; Other Information: PMCID: PMC2335077; PMID: 17554170; PUBLISHER-ID: fw5127; OAI: oai:pubmedcentral.nih.gov:2335077; Copyright (c) International Union of Crystallography 2007; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
- Subject:
- 75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; CRYSTALLIZATION; CRYSTALS; DIFFUSION; MOLECULAR WEIGHT; MOLECULES; PHOSPHATES; RESOLUTION; SOLVENTS; SPACE GROUPS; X-RAY DIFFRACTION
Citation Formats
Chen, Chung-Der, Huang, Tien-Feng, Lin, Chih-Hao, Guan, Hong-Hsiang, Hsieh, Yin-Cheng, Institute of Bioinformatics and Structural Biology, National Tsing-Hua University, Hsinchu 30013,Taiwan, Lin, Yi-Hung, Huang, Yen-Chieh, Liu, Ming-Yih, Chang, Wen-Chang, Chen, Chun-Jung, and Life Science Group, Research Division, National Synchrotron Radiation Research Center, Hsinchu 30076,Taiwan. Purification, crystallization and preliminary X-ray crystallographic analysis of branched-chain aminotransferase from Deinococcus radiodurans. United Kingdom: N. p., 2007.
Web. doi:10.1107/S1744309107020842.
Chen, Chung-Der, Huang, Tien-Feng, Lin, Chih-Hao, Guan, Hong-Hsiang, Hsieh, Yin-Cheng, Institute of Bioinformatics and Structural Biology, National Tsing-Hua University, Hsinchu 30013,Taiwan, Lin, Yi-Hung, Huang, Yen-Chieh, Liu, Ming-Yih, Chang, Wen-Chang, Chen, Chun-Jung, & Life Science Group, Research Division, National Synchrotron Radiation Research Center, Hsinchu 30076,Taiwan. Purification, crystallization and preliminary X-ray crystallographic analysis of branched-chain aminotransferase from Deinococcus radiodurans. United Kingdom. https://doi.org/10.1107/S1744309107020842
Chen, Chung-Der, Huang, Tien-Feng, Lin, Chih-Hao, Guan, Hong-Hsiang, Hsieh, Yin-Cheng, Institute of Bioinformatics and Structural Biology, National Tsing-Hua University, Hsinchu 30013,Taiwan, Lin, Yi-Hung, Huang, Yen-Chieh, Liu, Ming-Yih, Chang, Wen-Chang, Chen, Chun-Jung, and Life Science Group, Research Division, National Synchrotron Radiation Research Center, Hsinchu 30076,Taiwan. 2007.
"Purification, crystallization and preliminary X-ray crystallographic analysis of branched-chain aminotransferase from Deinococcus radiodurans". United Kingdom. https://doi.org/10.1107/S1744309107020842.
@article{osti_22360344,
title = {Purification, crystallization and preliminary X-ray crystallographic analysis of branched-chain aminotransferase from Deinococcus radiodurans},
author = {Chen, Chung-Der and Huang, Tien-Feng and Lin, Chih-Hao and Guan, Hong-Hsiang and Hsieh, Yin-Cheng and Institute of Bioinformatics and Structural Biology, National Tsing-Hua University, Hsinchu 30013,Taiwan and Lin, Yi-Hung and Huang, Yen-Chieh and Liu, Ming-Yih and Chang, Wen-Chang and Chen, Chun-Jung and Life Science Group, Research Division, National Synchrotron Radiation Research Center, Hsinchu 30076,Taiwan},
abstractNote = {The crystallization of branched-chain aminotransferase from D. radiodurans is described. 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 P2{sub 1}2{sub 1}2{sub 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%.},
doi = {10.1107/S1744309107020842},
url = {https://www.osti.gov/biblio/22360344},
journal = {Acta Crystallographica. Section F},
issn = {1744-3091},
number = Pt 6,
volume = 63,
place = {United Kingdom},
year = {Fri Jun 01 00:00:00 EDT 2007},
month = {Fri Jun 01 00:00:00 EDT 2007}
}