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

doi:10.1107/S0907444998009019

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 journal › Article › peer-review

7 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 language	English
Pages (from-to)	294-296
Number of pages	3
Journal	Acta Crystallographica Section D: Biological Crystallography
Volume	55
Issue number	1
DOIs	https://doi.org/10.1107/S0907444998009019
Publication status	Published - 1999 Jan 1
Externally published	Yes

ASJC Scopus subject areas

Structural Biology

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

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

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AU - Lee, Dae Sil

AU - Suh, Se Won

PY - 1999/1/1

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AB - 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.

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

Abstract

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