Title | Crystallization and preliminary crystallographic studies of the recombinant L-N-carbamoylase from Geobacillus stearothermophilus CECT43. |
Publication Type | Journal Article |
Year of Publication | 2008 |
Authors | Martinez-Rodriguez, S., A. Garcia-Pino, F. Javier Las Heras-Vázquez, J. María Clemente-Jiménez, F. Rodríguez-Vico, R. Loris, J. Ma García-Ruiz, and J. Antonio Gavira |
Journal | Acta Crystallogr Sect F Struct Biol Cryst Commun |
Volume | 64 |
Issue | Pt 12 |
Pagination | 1135-8 |
Date Published | 2008 Dec 1 |
ISSN | 1744-3091 |
Keywords | Amidohydrolases, Bacterial Proteins, Cloning, Molecular, Crystallization, Crystallography, X-Ray, Geobacillus stearothermophilus, Molecular Weight, Recombinant Proteins |
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. |
DOI | 10.1107/S1744309108034830 |
Alternate Journal | Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. |
PubMed ID | 19052368 |
PubMed Central ID | PMC2593709 |
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