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

ABSTRACT: ?-Mannosidase (EC 3.2.1.25) is an important exoglycosidase specific for the hydrolysis of terminal ?-linked mannoside in various oligomeric saccharide structures. ?-Mannosidase from Aspergillus niger was expressed in Pichia pastoris and purified to clear homogeneity. ?-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, ?=108.20, ?=101.51, ?=103.20°. The parameters derived from the data collection indicate the presence of one molecule in the asymmetric unit.

SUBMITTER: Demo G

PROVIDER: S-EPMC3606576 | biostudies-literature | 2013 Mar

REPOSITORIES: biostudies-literature

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

Demo Gabriel G Fliedrová Barbora B Weignerová Lenka L Wimmerová Michaela M

Acta crystallographica. Section F, Structural biology and crystallization communications 20130223 Pt 3

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 ...[more]

PMID: 23519806

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Crystallization and preliminary X-ray diffraction data of ?-galactosidase from Aspergillus niger.

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