Expression, purification, crystallization and preliminary X-ray analysis of alpha-L-arabinofuranosidase B from Aspergillus kawachii.
Alpha-L-Arabinofuranosidase (EC 3.2.1.55) is one of the hemicellulases that cleave the glycosidic bonds between L-arabinofuranoside side chains and various oligosaccharides. In this study, the first crystallization and preliminary X-ray analysis of alpha-L-arabinofuranosidase B from Aspergillus kawachii IFO4308 (AkAbfB), a family 54 glycoside hydrolase, is described. Recombinant AkAbfB was expressed in Escherichia coli and Pichia pastoris. The native crystals of recombinant AkAbfB produced by P. pastoris belong to the orthorhombic space group P2(1)2(1)2(1) (unit-cell parameters a = 39.5, b = 98.2, c = 144.0 A) and diffracted X-rays to a resolution of 1.82 A.
Miyanaga
Akimasa
A
Department of Biotechnology, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan.
Koseki
Takuya
T
Matsuzawa
Hiroshi
H
Wakagi
Takayoshi
T
Shoun
Hirofumi
H
Fushinobu
Shinya
S
D001230:Aspergillus / Q000201:enzymology*; D003460:Crystallization; D018360:Crystallography, X-Ray; D015870:Gene Expression; D006026:Glycoside Hydrolases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism
D006026:Glycoside Hydrolases; C019713:alpha-N-arabinofuranosidase