Open AccessCrystallization and preliminary X‐ray crystallographic analysis of recombinant β‐mannosidase from Aspergillus niger
Author(s) -
Demo Gabriel,
Fliedrová Barbora,
Weignerová Lenka,
Wimmerová Michaela
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309113002522
Subject(s) - aspergillus niger , pichia pastoris , crystallization , mannosidase , recombinant dna , hydrolysis , chemistry , exoglycosidase , mannose , crystallography , biochemistry , organic chemistry , glycoprotein , gene , glycan
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 P 1, 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.