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Title 

A thermostable xylose isomerase from Thermus thermophilus: biochemical characterization, crystallization, and preliminary X-ray analyses

Authors 

Chang Soo ChangByoung Chul ParkDae Sil LeeSe Won Suh

Publisher 

Springer Verlag (Germany)

Issue Date 

1998

Citation 

Journal of Biochemistry and Molecular Biology, vol. 31, no. 6, pp. 600-603

Keywords 

crystallizationthermostable enzymethermus thermopilusxylose isomerase

Abstract 

A highly thermostable xylose isomerase from Thermus thermophilus has been expressed in Escherichia coli and crystallized. The purified enzyme shows its optimum temperature at 90°C. It has been crystallized at room temperature using polyethylene glycol 4000 as the precipitant. The crystal belongs to the orthorhombic space group P212121, with unit cell parameters of a = 73.34 ?, b = 144.05 ?, c = 155.07 ?. The presence of one molecule of tetrameric xylose isomerase in the asymmetric unit gives a crystal volume per protein mass (Vm) of 2.32 ?3/Da and the solvent content of 47.0% by volume. The diffraction pattern extends to 1.9 ? Bragg spacing with synchrotron radiation and a set of native data has been collected to 2.3 ?.

ISSN 

1225-8687

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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