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- W2053643911 abstract "Xylanases (EC 3.2.1.8) catalyze the hydrolysis of β-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 Å, β = 131.2°, and diffract to better than 2.2 Å resolution." @default.
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- W2053643911 date "2005-07-08" @default.
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- W2053643911 title "Crystallization and preliminary X-ray study of a family 10 alkali-thermostable xylanase from alkalophilic<i>Bacillus</i>sp. strain NG-27" @default.
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- W2053643911 doi "https://doi.org/10.1107/s1744309105020518" @default.
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