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

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-α-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 Å. The crystals belonged to space group P2₁2₁2, with unit-cell parameters a = 103.2, b = 211.7, c = 43.1 Å and two subunits in the asymmetric unit.