Crystallization and preliminary X-ray crystallographic analysis of recombinant β-mannosidase from Aspergillus niger
Language English Country England, Great Britain Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
23519806
PubMed Central
PMC3606576
DOI
10.1107/s1744309113002522
PII: S1744309113002522
Knihovny.cz E-resources
- Keywords
- Aspergillus niger, β-mannosidase,
- 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
- Names of Substances
- beta-Mannosidase MeSH
- Fungal Proteins MeSH
- Mannose MeSH
- Recombinant Proteins 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.
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