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Crystallization and Preliminary X-ray Diffraction Analysis of Crystals of Thermoascus aurantiacus Xylanase

Viswamitra, MA and Bhanumoorthy, P and Ramakumar, S and Manjula, MV and Vithayathil, PJ and Murthy, SK and Naren, AP (1993) Crystallization and Preliminary X-ray Diffraction Analysis of Crystals of Thermoascus aurantiacus Xylanase. In: Journal of Molecular Biology, 232 (3). pp. 987-988.

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Official URL: http://dx.doi.org/10.1006/jmbi.1993.1444

Abstract

Crystals suitable for high resolution X-ray diffraction analysis have been grown of the 29,774-Da protein, xylanase (1,-4-beta-xylan xylanohydrolase EC 3.2.1.8) from the thermophilic fungus Thermoascus aurantiacus. This protein, an endoxylanase demonstrates the hydrolysis of β-(1-4)-Image -xylose linkage in xylans and crystallizes as monoclinic pinacoids in the presence of ammonium sulphate buffered at pH 6·5, and also with neutral polyethylene glycol 6000. The crystals belong to space group P 21 and have cell dimensions, a = 41·2 Å, b = 67·76 Å, c = 51·8 Å; β = 113·2°.

Item Type: Editorials/Short Communications
Additional Information: Copyright of this article belongs to Elsevier Science.
Keywords: Thermoascus aurantiacus;crystallization;X-ray crystallography;Xylanase.
Department/Centre: Division of Biological Sciences > Biochemistry
Division of Physical & Mathematical Sciences > Physics
Date Deposited: 03 Feb 2011 08:51
Last Modified: 03 Feb 2011 08:51
URI: http://eprints.iisc.ernet.in/id/eprint/35387

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