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

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dc.contributor.authorChang Soo Chang-
dc.contributor.authorH K Song-
dc.contributor.authorByoung Chul Park-
dc.contributor.authorDae Sil Lee-
dc.contributor.authorSe Won Suh-
dc.date.accessioned2017-04-19T08:56:17Z-
dc.date.available2017-04-19T08:56:17Z-
dc.date.issued1999-
dc.identifier.citationActa Crystallographica. Section D, Biological Crystallography,55,1,294,296ko
dc.identifier.issn0907-4449-
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/4790-
dc.description.abstractA 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.-
dc.publisherInt Union Crystallography-
dc.titleA thermostable xylose isomerase from Thermus caldophilus: biochemical charaterization, crystallization and preliminary X-ray analysis-
dc.title.alternativeA thermostable xylose isomerase from Thermus caldophilus: biochemical charaterization, crystallization and preliminary X-ray analysis-
dc.typeArticle-
dc.citation.titleActa Crystallographica Section D-Biological Crystallography-
dc.citation.number1-
dc.citation.endPage296-
dc.citation.startPage294-
dc.citation.volume55-
dc.contributor.affiliatedAuthorByoung Chul Park-
dc.contributor.affiliatedAuthorDae Sil Lee-
dc.contributor.alternativeName장창수-
dc.contributor.alternativeName송현규-
dc.contributor.alternativeName박병철-
dc.contributor.alternativeName이대실-
dc.contributor.alternativeName서세원-
dc.identifier.bibliographicCitationActa Crystallographica Section D-Biological Crystallography, vol. 55, no. 1, pp. 294-296-
dc.identifier.doi10.1107/S0907444998009019-
dc.description.journalClassY-
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