Crystallization and preliminary X-ray analysis of a truncated family A alkaline endoglucanase isolated from Bacillus sp. KSM-635.
The catalytic domain of an alkaline endo-1,4-beta-glucanase (family A) isolated from Bacillus sp. KSM-635 (Mr = 40.2 kDa) was crystallized using the hanging drop vapor diffusion method. Two different crystal forms were obtained. Form 2 crystals (trigonal space group R3 with cell dimensions of a = b = 111.9 and c = 207.1 angstroms in a hexagonal lattice) were found to be more stable than form 1 ones upon X-ray irradiation. A full data set for form 2 crystals has been collected up to 3.3 angstroms resolution.
Shirai
T
T
Department of Biotechnology and Biomaterial Chemistry, Graduate School of Engineering, Nagoya University.
Yamane
T
T
Hidaka
T
T
Kuyama
K
K
Suzuki
A
A
Ashida
T
T
Ozaki
K
K
Ito
S
S
D000595:Amino Acid Sequence; D001407:Bacillus / Q000201:enzymology*; D002384:Catalysis; D002480:Cellulase / Q000737:chemistry* / Q000378:metabolism; D018360:Crystallography, X-Ray; D008969:Molecular Sequence Data; D017386:Sequence Homology, Amino Acid
D002480:Cellulase