Crystallization and preliminary X-ray analysis of an arabinoxylan arabinofuranohydrolase from Bacillus subtilis.
Arabinoxylan arabinofuranohydrolases (AXH) are alpha-L-arabinofuranosidases (EC 3.2.1.55) that specifically hydrolyse the glycosidic bond between arabinofuranosyl substituents and xylopyranosyl residues from arabinoxylan, hence their name. In this study, the crystallization and preliminary X-ray analysis of the AXH from Bacillus subtilis, a glycoside hydrolase belonging to family 43, is described. Purified recombinant AXH crystallized in the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 68.7, b = 73.7, c = 106.5 A. X-ray diffraction data were collected to a resolution of 1.55 A.
Laboratory for Biocrystallography, Katholieke Universiteit Leuven, Herestraat 49, O&N II bus 822, 3000 Leuven, Belgium.
Elien
E
Vandermarliere
Tine M
TM
Bourgois
Steven
S
Van Campenhout
Sergei V
SV
Strelkov
Guido
G
Volckaert
Jan A
JA
Delcour
Christophe M
CM
Courtin
Anja
A
Rabijns
D001412:Bacillus subtilis / Q000201:enzymology*; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D003460:Crystallization; D018360:Crystallography, X-Ray; D006026:Glycoside Hydrolases / Q000737:chemistry* / Q000378:metabolism; D013379:Substrate Specificity; D014990:Xylans / Q000737:chemistry* / Q000378:metabolism
D001426:Bacterial Proteins; D014990:Xylans; C085118:arabinoxylan; D006026:Glycoside Hydrolases; C019713:alpha-N-arabinofuranosidase