Purification, crystallization and preliminary X-ray crystallographic analysis of branched-chain aminotransferase from Deinococcus radiodurans

Chung Der Chen; Tien Feng Huang; Chih Hao Lin; Hong Hsiang Guan; Yin Cheng Hsieh; Yi Hung Lin; Yen Chieh Huang; Ming Yih Liu; Wen Chang Chang; Chun Jung Chen

doi:10.1107/S1744309107020842

Purification, crystallization and preliminary X-ray crystallographic analysis of branched-chain aminotransferase from Deinococcus radiodurans

Chung Der Chen, Tien Feng Huang, Chih Hao Lin, Hong Hsiang Guan, Yin Cheng Hsieh, Yi Hung Lin, Yen Chieh Huang, Ming Yih Liu, Wen Chang Chang, Chun Jung Chen

Research output: Contribution to journal › Article › peer-review

2 Citations (Scopus)

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 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%.

Original language	English
Pages (from-to)	492-494
Number of pages	3
Journal	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Volume	63
Issue number	6
DOIs	https://doi.org/10.1107/S1744309107020842
Publication status	Published - May 5 2007
Externally published	Yes

Keywords

Branched-chain amino-acid aminotransferase
Deinococcus radiodurans

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Genetics
Condensed Matter Physics

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10.1107/S1744309107020842

Cite this

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

Purification, crystallization and preliminary X-ray crystallographic analysis of branched-chain aminotransferase from Deinococcus radiodurans. / Chen, Chung Der; Huang, Tien Feng; Lin, Chih Hao et al.
In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 63, No. 6, 05.05.2007, p. 492-494.

Research output: Contribution to journal › Article › peer-review

Chen, CD, Huang, TF, Lin, CH, Guan, HH, Hsieh, YC, Lin, YH, Huang, YC, Liu, MY, Chang, WC & Chen, CJ 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, vol. 63, no. 6, pp. 492-494. https://doi.org/10.1107/S1744309107020842

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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 {\AA} 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 {\AA}. Preliminary analysis indicates the presence of two DrBCAT molecules in the asymmetric unit, with a solvent content of 47.52%.",

keywords = "Branched-chain amino-acid aminotransferase, Deinococcus radiodurans",

author = "Chen, {Chung Der} and Huang, {Tien Feng} and Lin, {Chih Hao} and Guan, {Hong Hsiang} and Hsieh, {Yin Cheng} and Lin, {Yi Hung} and Huang, {Yen Chieh} and Liu, {Ming Yih} and Chang, {Wen Chang} and Chen, {Chun Jung}",

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doi = "10.1107/S1744309107020842",

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AU - Chen, Chung Der

AU - Huang, Tien Feng

AU - Lin, Chih Hao

AU - Guan, Hong Hsiang

AU - Hsieh, Yin Cheng

AU - Lin, Yi Hung

AU - Huang, Yen Chieh

AU - Liu, Ming Yih

AU - Chang, Wen Chang

AU - Chen, Chun Jung

PY - 2007/5/5

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N2 - 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%.

AB - 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%.

KW - Branched-chain amino-acid aminotransferase

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Purification, crystallization and preliminary X-ray crystallographic analysis of branched-chain aminotransferase from Deinococcus radiodurans

Abstract

Keywords

ASJC Scopus subject areas

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