Crystallization and preliminary crystallographic studies of the recombinant L-N-carbamoylase from Geobacillus stearothermophilus CECT43.

TitleCrystallization and preliminary crystallographic studies of the recombinant L-N-carbamoylase from Geobacillus stearothermophilus CECT43.
Publication TypeJournal Article
Year of Publication2008
AuthorsMartinez-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
JournalActa Crystallogr Sect F Struct Biol Cryst Commun
Volume64
IssuePt 12
Pagination1135-8
Date Published2008 Dec 1
ISSN1744-3091
KeywordsAmidohydrolases, 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.

DOI10.1107/S1744309108034830
Alternate JournalActa Crystallogr. Sect. F Struct. Biol. Cryst. Commun.
PubMed ID19052368
PubMed Central IDPMC2593709