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

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2 Citations (Scopus)


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 languageEnglish
Pages (from-to)492-494
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Issue number6
Publication statusPublished - May 5 2007
Externally publishedYes



  • Branched-chain amino-acid aminotransferase
  • Deinococcus radiodurans

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics

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