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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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 |
|---|---|
| Publication: | Acta Crystallographica Section F: Structural Biology and Crystallization Communications |
| Publisher: | Blackwell Publishing |
| Additional Information: | Copyright for this article belongs to Blackwell Publishing. |
| Keywords: | xylanases;alkali-thermostable proteins |
| Department/Centre: | Division of Information Sciences (Doesn't exist now) > BioInformatics Centre Division of Physical & Mathematical Sciences > Physics |
| Date Deposited: | 10 Nov 2005 |
| Last Modified: | 27 Aug 2008 11:32 |
| URI: | http://eprints.iisc.ac.in/id/eprint/3976 |
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