title: Crystallization and preliminary crystallographic analysis of peptide-N4-(N-acetyl-beta-D-glucosaminyl)asparagine amidase PNGase F.
abstract: PNGase F is an amidase that hydrolyzes the beta-aspartylglucosylamine bond of asparagine-linked glycopeptides and glycoproteins. Enzymatic activity of PNGase F requires the recognition of both the peptide and the carbohydrate moiety. Crystals of PNGase F were grown by sitting drop vapor diffusion methods at 10 degrees C. The precipitating buffer contains both polyethylene glycol 3350 and (NH4)2SO4 in sodium acetate buffer at pH 4.3. The crystals belong to the orthorhombic space group C222(1) with cell dimensions: a = 87.16 A, b = 125.10 A, c = 79.33 A and diffract to 1.8 A resolution.
authors.affiliation: Wadsworth Center, New York State Department of Health, Albany 12201-0509.
authors.forename: P
authors.initials: P
authors.lastname: Kuhn
authors.forename: A L
authors.initials: AL
authors.lastname: Tarentino
authors.forename: T H
authors.initials: TH
authors.lastname: Plummer
authors.forename: P
authors.initials: P
authors.lastname: Van Roey
mesh_terms: D000581:Amidohydrolases / Q000737:chemistry* / Q000302:isolation & purification; D003460:Crystallization; D003461:Crystallography; D005417:Flavobacterium / Q000201:enzymology; D043524:Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase
chemical_list: D000581:Amidohydrolases; D043524:Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase