A thermostable xylose isomerase from Thermus caldophilus: Biochemical characterization, crystallization and preliminary x-ray analysis

Changsoo Chang, Hyun Kyu Song, Byung Chul Park, Dae Sil Lee, Se Won Suh

Research output: Contribution to journalArticle

5 Citations (Scopus)

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 Å. 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 Å D-1 and a solvent content of 41% by volume. The crystals initially showed diffraction to 1.7 Å Bragg spacing with synchrotron X-rays, and a set of native data extending to 2.3 Å resolution has been collected.

Original languageEnglish
Pages (from-to)294-296
Number of pages3
JournalActa Crystallographica Section D: Biological Crystallography
Volume55
Issue number1
Publication statusPublished - 1999 Jan 1
Externally publishedYes

ASJC Scopus subject areas

  • Clinical Biochemistry
  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Biophysics
  • Condensed Matter Physics
  • Structural Biology

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