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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,
Jazyk angličtina Země Anglie, Velká Británie
Typ dokumentu časopisecké články, práce podpořená grantem
NLK
Free Medical Journals
od 2005 do 2013
PubMed Central
od 2005 do 2013
Europe PubMed Central
od 2005 do 2013
- 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
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.
Citace poskytuje Crossref.org
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