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Crystallization and preliminary X-ray characterization of a thermostable low-molecularweight 1,4-$\beta$-D-glucan glucohydrolase from an alkalothermophilic Thermomonospora sp.

Manikandan, K and Jagtap, S and Rao, M and Ramakumar, S (2006) Crystallization and preliminary X-ray characterization of a thermostable low-molecularweight 1,4-$\beta$-D-glucan glucohydrolase from an alkalothermophilic Thermomonospora sp. In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 62 (4). pp. 385-357.

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Abstract

Cellulases catalyze the hydrolysis of $\beta-1,4$glycosidic linkages within cellulose, the most abundant organic polymer on earth. The cellulase (TSC; EC 3.2.1.4) from an alkalothermophilic Thermomonospora sp. has a low molecular weight of 14.2 kDa. It is optimally active at 323 K and stable over the wide pH range of 5-9. Moreover, it has bifunctional activity against cellulose and xylan polymers. In this study, TSC was purified from the native source and crystallized by the hanging-drop vapour-diffusion method. The crystals belong to the orthorhombic space group $P2_12_12_1$, with unit-cell parameters a = 49.9, b = 79.5, c = 99.7 $\AA$, and diffract to better than 2.3 $\AA$ resolution.

Item Type: Journal Article
Additional Information: The copyright of this article belongs to International Union of Crystallography.
Keywords: Sequence-Based Classification;Hydroclases;Cellulases
Department/Centre: Division of Physical & Mathematical Sciences > Physics
Date Deposited: 25 Apr 2006
Last Modified: 19 Sep 2010 04:25
URI: http://eprints.iisc.ernet.in/id/eprint/6423

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