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A thermostable xylose isomerase from Thermus caldophilus: biochemical characterization, crystallization and preliminary X-ray analysis.
Acta Crystallogr D Biol Crystallogr. 1999 Jan; 55(Pt 1):294-6.AC

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 (Vm) of 2.1 A3 Da-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.

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Authors+Show Affiliations

Chang C
Department of Chemistry, College of Natural Sciences, Seoul National University, Seoul 151-742, Korea.
Song HK
No affiliation info available
Park BC
No affiliation info available
Lee DS
No affiliation info available
Suh SW
No affiliation info available

MeSH

Aldose-Ketose IsomerasesCrystallizationCrystallography, X-RayEnzyme StabilityEscherichia coliGene ExpressionMetalsRecombinant ProteinsTemperatureThermus

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

10089429

Citation

Chang, C, et al. "A Thermostable Xylose Isomerase From Thermus Caldophilus: Biochemical Characterization, Crystallization and Preliminary X-ray Analysis." Acta Crystallographica. Section D, Biological Crystallography, vol. 55, no. Pt 1, 1999, pp. 294-6.
Chang C, Song HK, Park BC, et al. A thermostable xylose isomerase from Thermus caldophilus: biochemical characterization, crystallization and preliminary X-ray analysis. Acta Crystallogr D Biol Crystallogr. 1999;55(Pt 1):294-6.
Chang, C., Song, H. K., Park, B. C., Lee, D. S., & Suh, S. W. (1999). A thermostable xylose isomerase from Thermus caldophilus: biochemical characterization, crystallization and preliminary X-ray analysis. Acta Crystallographica. Section D, Biological Crystallography, 55(Pt 1), 294-6.
Chang C, et al. A Thermostable Xylose Isomerase From Thermus Caldophilus: Biochemical Characterization, Crystallization and Preliminary X-ray Analysis. Acta Crystallogr D Biol Crystallogr. 1999;55(Pt 1):294-6. PubMed PMID: 10089429.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - A thermostable xylose isomerase from Thermus caldophilus: biochemical characterization, crystallization and preliminary X-ray analysis. AU - Chang,C, AU - Song,H K, AU - Park,B C, AU - Lee,D S, AU - Suh,S W, Y1 - 1999/01/01/ PY - 1998/06/05/received PY - 1998/07/02/accepted PY - 1999/3/25/pubmed PY - 2000/6/23/medline PY - 1999/3/25/entrez SP - 294 EP - 6 JF - Acta crystallographica. Section D, Biological crystallography JO - Acta Crystallogr D Biol Crystallogr VL - 55 IS - Pt 1 N2 - 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 (Vm) of 2.1 A3 Da-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. SN - 0907-4449 UR - https://www.unboundmedicine.com/medline/citation/10089429/A_thermostable_xylose_isomerase_from_Thermus_caldophilus:_biochemical_characterization_crystallization_and_preliminary_X_ray_analysis_ L2 - http://scripts.iucr.org/cgi-bin/paper?S0907444998009019 DB - PRIME DP - Unbound Medicine ER -