Open AccessCrystallization and diffraction analysis of β‐ N ‐acetylhexosaminidase from Aspergillus oryzae
Author(s) -
Vaněk Ondřej,
Brynda Jiří,
Hofbauerová Kateřina,
Kukačka Zdeněk,
Pachl Petr,
Bezouška Karel,
Řezáčová Pavlína
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309111004945
Subject(s) - aspergillus oryzae , crystallization , aspergillus , crystallography , chemistry , materials science , microbiology and biotechnology , biology , biochemistry , enzyme , organic chemistry
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.