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Crystallization and preliminary X-ray study of a family 10 alkali-thermostable xylanase from alkalophilic Bacillus sp. strain NG-27

Manikandan, K and Bhardwaj, Amit and Ghosh, Amit and Reddy, VS and Ramakumar, S (2005) Crystallization and preliminary X-ray study of a family 10 alkali-thermostable xylanase from alkalophilic Bacillus sp. strain NG-27. In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 61 (Part 8). pp. 747-749.

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Abstract

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-thermo stable 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 Angstrom, \beta = 131.2 Angstrom, and diffract to better than 2.2 Angstrom resolution.

Item Type: Journal Article
Additional Information: Copyright for this article belongs to Blackwell Publishing.
Keywords: xylanases;alkali-thermostable proteins
Department/Centre: Division of Information Sciences > BioInformatics Centre
Division of Physical & Mathematical Sciences > Physics
Date Deposited: 10 Nov 2005
Last Modified: 27 Aug 2008 11:32
URI: http://eprints.iisc.ernet.in/id/eprint/3976

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