Crystallization and preliminary X-ray characterization of a thermostable low-molecular-weight 1,4-beta-D-glucan glucohydrolase from an alkalothermophilic Thermomonospora sp.
Cellulases catalyze the hydrolysis of beta-1,4-glycosidic linkages within cellulose, the most abundant organic polymer on earth. The cellulase (TSC; EC 3.2.1.4) from an alkalothermophilic Thermomonospora sp. has a low molecular weight of 14.2 kDa. It is optimally active at 323 K and stable over the wide pH range of 5-9. Moreover, it has bifunctional activity against cellulose and xylan polymers. In this study, TSC was purified from the native source and crystallized by the hanging-drop vapour-diffusion method. The crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 49.9, b = 79.5, c = 99.7 angstroms, and diffract to better than 2.3 angstroms resolution.
Manikandan
K
K
Department of Physics, Indian Institute of Science, Bangalore 560 012, India.
Jagtap
S
S
Rao
M
M
Ramakumar
S
S
D000192:Actinomycetales / Q000201:enzymology*; D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D003460:Crystallization; D018360:Crystallography, X-Ray; D004795:Enzyme Stability; D044643:Glucan 1,4-beta-Glucosidase / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D013816:Thermodynamics; D014961:X-Ray Diffraction
D001426:Bacterial Proteins; D044643:Glucan 1,4-beta-Glucosidase