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  • Title: Crystallization and preliminary crystallographic studies of the recombinant L-N-carbamoylase from Geobacillus stearothermophilus CECT43.
    Author: Martínez-Rodríguez S, García-Pino A, Las Heras-Vázquez FJ, Clemente-Jiménez JM, Rodríguez-Vico F, Loris R, García-Ruiz JM, Gavira JA.
    Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun; 2008 Dec 01; 64(Pt 12):1135-8. PubMed ID: 19052368.
    Abstract:
    N-Carbamoyl-L-amino-acid amidohydrolases (L-N-carbamoylases; EC 3.5.1.87) hydrolyze the carbon-nitrogen bond of the ureido group in N-carbamoyl-L-alpha-amino acids. These enzymes are commonly used in the production of optically pure natural and non-natural L-amino acids using the ;hydantoinase process'. Recombinant L-N-carbamoylase from Geobacillus stearothermophilus CECT43 has been expressed, purified and crystallized by hanging-drop vapour diffusion. X-ray data were collected to a resolution of 2.75 A. The crystals belonged to space group P2(1)2(1)2, with unit-cell parameters a = 103.2, b = 211.7, c = 43.1 A and two subunits in the asymmetric unit.
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