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

Authors :: Neumann S
Granzin J
Kula MR
Labahn J
Source :: Acta crystallographica. Section D, Biological crystallography [Acta Crystallogr D Biol Crystallogr] 2002 Feb; Vol. 58 (Pt 2), pp. 333-5. Date of Electronic Publication: 2002 Jan 24.
Publication Year :: 2002
Abstract: 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.

Subjects :: Amidohydrolases genetics
Amino Acid Sequence
Crystallization
Crystallography, X-Ray
Molecular Sequence Data
Protein Conformation
Recombinant Proteins chemistry
Recombinant Proteins genetics
Amidohydrolases chemistry
Stenotrophomonas maltophilia enzymology

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