Crystallization and diffraction analysis of [beta]-N-acetylhexosaminidase from Aspergillus oryzae

Journal Article · Tue May 08 00:00:00 EDT 2012 · Acta Crystallogr. F

DOI:https://doi.org/10.1107/S1744309111004945· OSTI ID:1034543

Vanek, Ondrej; Brynd, Jirí; Hofbauerová, Katerina; Kukack, Zdenek; Pachl, Petr; Bezouska, Karel; Rezácová, Pavlína ^[1]

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1. Czech Academy

Fungal {beta}-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 vapor-diffusion method. Diffraction data from two crystal forms (primitive monoclinic and primitive tetragonal) were collected to resolutions of 3.2 and 2.4 {angstrom}, 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.

• Research Organization: Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
• Sponsoring Organization: FOREIGN
• OSTI ID: 1034543
• Journal Information: Acta Crystallogr. F, Vol. 67, Issue (4) ; 04, 2011; ISSN 1744-3091
• Country of Publication: United States
• Language: ENGLISH

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
60 APPLIED LIFE SCIENCES
AMINO ACID SEQUENCE
ASPERGILLUS
CRYSTALLIZATION
DIFFRACTION
ENZYMES
GLYCOPROTEINS
OLIGOSACCHARIDES
SYNTHESIS