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Crystallization and preliminary X-ray crystallographic analysis of recombinant β-mannosidase from Aspergillus niger
G. Demo, B. Fliedrová, L. Weignerová, M. Wimmerová,
Language English Country England, Great Britain
Document type Journal Article, Research Support, Non-U.S. Gov't
NLK
Free Medical Journals
from 2005 to 2013
PubMed Central
from 2005 to 2013
Europe PubMed Central
from 2005 to 2013
- MeSH
- Aspergillus niger chemistry enzymology MeSH
- beta-Mannosidase chemistry genetics MeSH
- Fungal Proteins chemistry genetics MeSH
- Crystallization MeSH
- Crystallography, X-Ray MeSH
- Mannose chemistry MeSH
- Pichia chemistry genetics MeSH
- Recombinant Proteins chemistry genetics MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
β-Mannosidase (EC 3.2.1.25) is an important exoglycosidase specific for the hydrolysis of terminal β-linked mannoside in various oligomeric saccharide structures. β-Mannosidase from Aspergillus niger was expressed in Pichia pastoris and purified to clear homogeneity. β-Mannosidase was crystallized in the presence of D-mannose and the crystal diffracted to 2.41 Å resolution. The crystal belonged to space group P1, with unit-cell parameters a=62.37, b=69.73, c=69.90 Å, α=108.20, β=101.51, γ=103.20°. The parameters derived from the data collection indicate the presence of one molecule in the asymmetric unit.
References provided by Crossref.org
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