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Crystallization and diffraction analysis of β‐ N ‐acetylhexosaminidase from Aspergillus oryzae

Crystallization and diffraction analysis of β‐ N ‐acetylhexosaminidase from Aspergillus oryzae 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Acta Crystallographica Section F Wiley

Crystallization and diffraction analysis of β‐ N ‐acetylhexosaminidase from Aspergillus oryzae

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References (28)

Publisher
Wiley
Copyright
International Union of Crystallography, 2011
ISSN
1744-3091
eISSN
1744-3091
DOI
10.1107/S1744309111004945
pmid
21505251
Publisher site
See Article on Publisher Site

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.

Journal

Acta Crystallographica Section FWiley

Published: Apr 1, 2011

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