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  • Title: Purification, crystallization and preliminary X-ray crystallographic analysis of branched-chain aminotransferase from Deinococcus radiodurans.
    Author: Chen CD, Huang TF, Lin CH, Guan HH, Hsieh YC, Lin YH, Huang YC, Liu MY, Chang WC, Chen CJ.
    Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun; 2007 Jun 01; 63(Pt 6):492-4. PubMed ID: 17554170.
    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%.
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