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.

PDF Structural_Biology_and_Crystallization_Communications.pdf Restricted to Registered users only Download (266kB) | Request a copy

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
Publication:	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Publisher:	International Union of Crystallography
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.ac.in/id/eprint/6423

Actions (login required)

View Item