1pvx

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Revision as of 01:03, 21 November 2007 by OCA (talk | contribs) (New page: left|200px<br /><applet load="1pvx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pvx, resolution 1.59Å" /> '''DO-1,4-BETA-XYLANASE...)
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File:1pvx.jpg


1pvx, resolution 1.59Å

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DO-1,4-BETA-XYLANASE, ROOM TEMPERATURE, PH 4.5

OverviewOverview

A highly thermostable xylanase isolated from the thermophilic fungus, Paecilomyces varioti has been crystallized by the vapour diffusion method., The isolation of this enzyme by crystallization directly from the culture, filtrate projects this fungus as an important source for large-scale, production of pure xylanase. The crystals belong to orthorhombic space, group P2(1)2(1)2(1) with the unit cell dimensions a = 38.48 A, b = 53.87 A, and c = 90.23 A. Four molecules occupy a volume of 187,039.4 A3 along with, 34% of solvent. The data collected with an area detector to the resolution, of 2.7 A were used to calculate the unit cell parameters and Matthews', constant. The optical behaviour of the crystal was studied at different, temperatures to understand its thermal stability.

About this StructureAbout this Structure

1PVX is a Single protein structure of sequence from Paecilomyces variotii. Active as Endo-1,4-beta-xylanase, with EC number 3.2.1.8 Full crystallographic information is available from OCA.

ReferenceReference

Crystallization and preliminary X-ray crystallographic studies of thermostable xylanase crystals isolated from Paecilomyces varioti., Eswaramoorthy S, Vithayathil PJ, Viswamitra MA, J Mol Biol. 1994 Nov 4;243(4):806-8. PMID:7966300

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