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Title | A thermostable xylose isomerase from Thermus thermophilus: biochemical characterization, crystallization, and preliminary X-ray analyses |
Authors | Chang Soo Chang; Byoung Chul Park; Dae Sil Lee; Se Won Suh |
Publisher | Springer Verlag (Germany) |
Issue Date | 1998 |
Citation | Journal of Biochemistry and Molecular Biology, vol. 31, no. 6, pp. 600-603 |
Keywords | crystallization; thermostable enzyme; thermus thermopilus; xylose isomerase |
Abstract | A highly thermostable xylose isomerase from Thermus thermophilus has been expressed in Escherichia coli and crystallized. The purified enzyme shows its optimum temperature at 90°C. It has been crystallized at room temperature using polyethylene glycol 4000 as the precipitant. The crystal belongs to the orthorhombic space group P212121, with unit cell parameters of a = 73.34 ?, b = 144.05 ?, c = 155.07 ?. The presence of one molecule of tetrameric xylose isomerase in the asymmetric unit gives a crystal volume per protein mass (Vm) of 2.32 ?3/Da and the solvent content of 47.0% by volume. The diffraction pattern extends to 1.9 ? Bragg spacing with synchrotron radiation and a set of native data has been collected to 2.3 ?. |
ISSN | 1225-8687 |
Appears in Collections | |
Registered Date |
2017-04-19 |
