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

O. Vaněk, J. Brynda, K. Hofbauerová, Z. Kukačka, P. Pachl, K. Bezouška, P. Rezáčová,

. 2011 ; 67 (Pt 4) : 498-503. [pub] 20110326

Jazyk angličtina Země Anglie, Velká Británie

Typ dokumentu časopisecké články, práce podpořená grantem, Research Support, U.S. Gov't, Non-P.H.S.

Perzistentní odkaz   https://www.medvik.cz/link/bmc12027611

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.

Citace poskytuje Crossref.org

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