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.
Neumann
Sebastian
S
Institut für Enzymtechnologie der Heinrich-Heine Universität im Forschungszentrum Jülich, D-52426 Jülich, Germany.
Granzin
Joachim
J
Kula
Maria-Regina
MR
Labahn
Jörg
J
D000581:Amidohydrolases / Q000737:chemistry* / Q000235:genetics; D000595:Amino Acid Sequence; D003460:Crystallization; D018360:Crystallography, X-Ray; D008969:Molecular Sequence Data; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D020615:Stenotrophomonas maltophilia / Q000201:enzymology*
D011994:Recombinant Proteins; D000581:Amidohydrolases