Crystallization and preliminary X-ray crystallographic analysis of recombinant β-mannosidase from Aspergillus niger
Jazyk angličtina Země Anglie, Velká Británie Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
23519806
PubMed Central
PMC3606576
DOI
10.1107/s1744309113002522
PII: S1744309113002522
Knihovny.cz E-zdroje
- Klíčová slova
- Aspergillus niger, β-mannosidase,
- MeSH
- Aspergillus niger chemie enzymologie MeSH
- beta-mannosidasa chemie genetika MeSH
- fungální proteiny chemie genetika MeSH
- krystalizace MeSH
- krystalografie rentgenová MeSH
- mannosa chemie MeSH
- Pichia chemie genetika MeSH
- rekombinantní proteiny chemie genetika MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- beta-mannosidasa MeSH
- fungální proteiny MeSH
- mannosa MeSH
- rekombinantní proteiny 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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