Crystallization and preliminary X-ray data of the recombinant peptide amidase from Stenotrophomonas maltophilia.

The peptide amidase from Stenotrophomonas maltophilia selectively hydrolyses the C-terminal amide bond in peptide amides. Crystals have been obtained by sitting-drop vapour diffusion from solution containing polyethylene glycol (PEG) 6000, HEPES pH 7.5, glycerine and sodium azide (NaN(3)). The crystals belong to the monoclinic space group P2(1), with unit-cell parameters a = 74.18, b = 62.60, c = 101.91 A, beta = 90 degrees. X-ray data from these crystals diffracted at the European Synchrotron Radiation Facility (ESRF, France) ID14-1 beamline to 1.4 A.