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 F: Structural Biology and Crystallization Communications, 61 (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-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 \AA, $_\beta$ = 131.2°, and diffract to better than 2.2 \AA resolution.

Item Type:	Journal Article
Publication:	Acta Crystallographica F: Structural Biology and Crystallization Communications
Publisher:	International Union of Crystallography
Additional Information:	Copyright of this article belongs to International Union of Crystallography.
Keywords:	xylanases;Alkali-thermostable proteins
Department/Centre:	Division of Physical & Mathematical Sciences > Physics
Date Deposited:	04 Apr 2007
Last Modified:	19 Sep 2010 04:37
URI:	http://eprints.iisc.ac.in/id/eprint/10579

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