Crystallization and preliminary X-ray study of a family 10 alkali-thermostable xylanase from alkalophilic Bacillus sp. strain NG-27.
Xylanases (EC 3.2.1.8) catalyze the hydrolysis of beta-1,4-glycosidic linkages within xylan, a major hemicellulose component in the biosphere. The extracellular endoxylanase (XylnA) from the alkalophilic Bacillus sp. strain NG-27 belongs to family 10 of the glycoside hydrolases. It is active at 343 K and pH 8.4. Moreover, it has attractive features from the point of view of utilization in the paper pulp, animal feed and baking industries since it is an alkali-thermostable protein. In this study, XylnA was purified from the native host source and crystallized by the hanging-drop vapour-diffusion method. The crystals belong to the monoclinic space group C2, with unit-cell parameters a = 174.5, b = 54.7, c = 131.5 A, beta = 131.2 degrees, and diffract to better than 2.2 A resolution.
Manikandan
K
K
Department of Physics, Indian Institute of Science, Bangalore 560 012, India.
Bhardwaj
Amit
A
Ghosh
Amit
A
Reddy
V S
VS
Ramakumar
S
S
D000468:Alkalies / Q000737:chemistry; D001407:Bacillus / Q000145:classification* / Q000201:enzymology*; D003460:Crystallization; D018360:Crystallography, X-Ray; D003625:Data Collection; D043364:Endo-1,4-beta Xylanases / Q000737:chemistry*; D004795:Enzyme Stability; D006863:Hydrogen-Ion Concentration
D000468:Alkalies; D043364:Endo-1,4-beta Xylanases