A thermostable xylose isomerase from Thermus caldophilus: biochemical charaterization, crystallization and preliminary X-ray analysis

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Title
A thermostable xylose isomerase from Thermus caldophilus: biochemical charaterization, crystallization and preliminary X-ray analysis
Author(s)
Chang Soo Chang; H K Song; Byoung Chul Park; Dae Sil Lee; Se Won Suh
Bibliographic Citation
Acta Crystallographica Section D-Biological Crystallography, vol. 55, no. 1, pp. 294-296
Publication Year
1999
Abstract
A highly thermostable xylose isomerase from Thermus caldophilus has been expressed in Escherichia coli. The purified enzyme has an optimum temperature of 363 K. It has been crystallized at room temperature using ammonium sulfate as a precipitant. The crystal belongs to the orthorhombic space group P212121, with unit-cell parameters a = 84.35, b = 123.60, c = 140.24 A. The presence of one molecule of tetrameric xylose isomerase in the asymmetric unit gives a crystal volume per protein mass (V(m)) of 2.1 A D-1 and a solvent content of 41% by volume. The crystals initially showed diffraction to 1.7 A Bragg spacing with synchrotron X-rays, and a set of native data extending to 2.3 A resolution has been collected.
ISSN
0907-4449
Publisher
Int Union Crystallography
DOI
http://dx.doi.org/10.1107/S0907444998009019
Type
Article
Appears in Collections:
Critical Diseases Diagnostics Convergence Research Center > 1. Journal Articles
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