Crystallization and preliminary X-ray diffraction analysis of crystals of Thermoascus aurantiacus Xylanase

Viswamitra, M.A. ; Bhanumoorthy, P. ; Ramakumar, S. ; Manjula, M.V. ; Vithayathil, P.J. ; Murthy, S.K. ; Naren, A.P. (1993) Crystallization and preliminary X-ray diffraction analysis of crystals of Thermoascus aurantiacus Xylanase Journal of Molecular Biology, 232 (3). pp. 987-988. ISSN 0022-2836

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Official URL: http://www.sciencedirect.com/science/article/pii/S...

Related 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)-d-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:Article
Source:Copyright of this article belongs to Elsevier Science.
Keywords:Thermoascus aurantiacus; Crystallization; X-ray Crystallography; Xylanase
ID Code:72767
Deposited On:03 Dec 2011 11:57
Last Modified:03 Dec 2011 11:57

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