Crystallization and preliminary X-ray diffraction analysis of the catalytic domain of Cex, an exo-beta-1,4-glucanase and beta-1,4-xylanase from the bacterium Cellulomonas fimi.
Single crystals of the catalytic domain of Cex, an exo-beta-1,4-glucanase and beta-1,4-xylanase from the cellulolytic bacterium Cellulomonas fimi, have been grown in the presence of polyethylene glycol 4000 using the vapour diffusion technique. The crystals, which diffract to better than 2.0 A resolution, belong to space group P4(1)2(1)2 or P4(3)2(1)2 and have cell constants: a = b = 88.21 A, c = 81.10 A; alpha = beta = gamma = 90 degrees.
Bedarkar
S
S
Ontario Cancer Institute, Toronto, Canada.
Gilkes
N R
NR
Kilburn
D G
DG
Kwan
E
E
Rose
D R
DR
Miller
R C
RC
Warren
R A
RA
Withers
S G
SG
D000192:Actinomycetales / Q000201:enzymology*; D003460:Crystallization; D043364:Endo-1,4-beta Xylanases; D044643:Glucan 1,4-beta-Glucosidase; D006026:Glycoside Hydrolases / Q000737:chemistry*; D014961:X-Ray Diffraction; D001617:beta-Glucosidase / Q000737:chemistry*
D006026:Glycoside Hydrolases; D001617:beta-Glucosidase; D044643:Glucan 1,4-beta-Glucosidase; D043364:Endo-1,4-beta Xylanases