A thermostable xylose isomerase from Thermus caldophilus: biochemical charaterization, crystallization and preliminary X-ray analysis
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- A thermostable xylose isomerase from Thermus caldophilus: biochemical charaterization, crystallization and preliminary X-ray analysis
- 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
- 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.
- Int Union Crystallography
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- Critical Diseases Diagnostics Convergence Research Center > 1. Journal Articles
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