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

Manikandan, K. ; Bhardwaj, Amit ; Ghosh, Amit ; Reddy, V. S. ; Ramakumar, S. (2005) Crystallization and preliminary x-ray study of a family 10 alkali thermostable xylanase from alkalophilic Bacillus sp. strain NG-27 Acta Crystallographica Section F, 61 (8). pp. 747-749. ISSN 1744-3091

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Official URL: http://onlinelibrary.wiley.com/doi/10.1107/S174430...

Related URL: http://dx.doi.org/10.1107/S1744309105020518

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.

Item Type:Article
Source:Copyright of this article belongs to John Wiley and Sons.
Keywords:Xylanases; Alkali-thermostable Proteins
ID Code:91877
Deposited On:25 May 2012 05:15
Last Modified:25 May 2012 05:15

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