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Title 

A thermostable xylose isomerase from Thermus caldophilus: biochemical charaterization, crystallization and preliminary X-ray analysis

Authors 

Chang Soo ChangH K SongByoung Chul ParkDae Sil LeeSe Won Suh

Publisher 

International Union of Crystallography

Issue Date 

1999

Citation 

Acta Crystallographica. Section D, Biological Crystallography, vol. 55, no. 1, pp. 294-296

Keywords 

isomerasexylose isomeraseAldose-Ketose IsomerasesThermusThermus caldophilus

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 (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.

Citation 

Acta Crystallographica. Section D, Biological Crystallography, 55(1): 294-296

ISSN 

0907-4449

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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