title: Crystallization and diffraction analysis of β-N-acetylhexosaminidase from Aspergillus oryzae.
abstract: Fungal β-N-acetylhexosaminidases are enzymes that are used in the chemoenzymatic synthesis of biologically interesting oligosaccharides. The enzyme from Aspergillus oryzae was produced and purified from its natural source and crystallized using the hanging-drop vapour-diffusion method. Diffraction data from two crystal forms (primitive monoclinic and primitive tetragonal) were collected to resolutions of 3.2 and 2.4 Å, respectively. Electrophoretic and quantitative N-terminal protein-sequencing analyses confirmed that the crystals are formed by a complete biologically active enzyme consisting of a glycosylated catalytic unit and a noncovalently attached propeptide.
authors.affiliation: Institute of Microbiology, Academy of Sciences of the Czech Republic, Vídeňská 1083, 14220 Prague, Czech Republic.
authors.forename: Ondřej
authors.initials: O
authors.lastname: Vaněk
authors.forename: Jiří
authors.initials: J
authors.lastname: Brynda
authors.forename: Kateřina
authors.initials: K
authors.lastname: Hofbauerová
authors.forename: Zdeněk
authors.initials: Z
authors.lastname: Kukačka
authors.forename: Petr
authors.initials: P
authors.lastname: Pachl
authors.forename: Karel
authors.initials: K
authors.lastname: Bezouška
authors.forename: Pavlína
authors.initials: P
authors.lastname: Rezáčová
mesh_terms: D001236:Aspergillus oryzae / Q000201:enzymology*; D020134:Catalytic Domain; D003460:Crystallization; D018360:Crystallography, X-Ray; D006031:Glycosylation; D001619:beta-N-Acetylhexosaminidases / Q000737:chemistry* / Q000378:metabolism
chemical_list: D001619:beta-N-Acetylhexosaminidases