Crystallization and preliminary X-ray crystallographic analysis of recombinant beta-mannosidase from Aspergillus niger

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F13%3A00066027" target="_blank" >RIV/00216224:14740/13:00066027 - isvavai.cz</a>
Result on the web
<a href="http://dx.doi.org/10.1107/S1744309113002522" target="_blank" >http://dx.doi.org/10.1107/S1744309113002522</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1107/S1744309113002522" target="_blank" >10.1107/S1744309113002522</a>

Result language
angličtina
Original language name
Crystallization and preliminary X-ray crystallographic analysis of recombinant beta-mannosidase from Aspergillus niger
Original language description
beta-Mannosidase (EC 3.2.1.25) is an important exoglycosidase specific for the hydrolysis of terminal beta-linked mannoside in various oligomeric saccharide structures. beta-Mannosidase from Asperigillus niger was expressed in Pichia pastoris and purified to clear homogeneity. beta-mannosidase was crystallized in the presence of D-mannose and the crystal diffracted to 2.41 A resolution. The crystal belonged to space group P1. Monomeric structure was observed in the asymmetric unit.
Czech name
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Czech description
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Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
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Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year
2013
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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