Send to:

Choose Destination
See comment in PubMed Commons below
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Apr 1;67(Pt 4):498-503. doi: 10.1107/S1744309111004945. Epub 2011 Mar 26.

Crystallization and diffraction analysis of β-N-acetylhexosaminidase from Aspergillus oryzae.

Author information

  • 1Institute of Microbiology, Academy of Sciences of the Czech Republic, Vídeňská 1083, 14220 Prague, Czech Republic.


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.

[PubMed - indexed for MEDLINE]
Free PMC Article
PubMed Commons home

PubMed Commons

How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for International Union of Crystallography Icon for PubMed Central
    Loading ...
    Write to the Help Desk