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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Cellulases catalyze the hydrolysis of $\beta-1,4$glycosidic linkages within cellulose, the most abundant organic polymer on earth. The cellulase (TSC; EC 188.8.131.52) 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.|
|Department/Centre:||Division of Physical & Mathematical Sciences > Physics|
|Date Deposited:||25 Apr 2006|
|Last Modified:||19 Sep 2010 04:25|
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