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Overexpression, crystallization and preliminary X-ray crystallographic analysis of a putative xylose isomerase from Bacteroides thetaiotaomicron

Authors
Cho, Jea-WonHan, Byeong-GuPark, Sang YounKim, Seung JunKim, Myoung-DongLee, Byung Il
Issue Date
Oct-2013
Publisher
WILEY-BLACKWELL
Keywords
Bacteroides thetaiotaomicron; BT0793; glucose isomerase; xylose isomerase
Citation
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS, v.69, pp.1127 - 1130
Journal Title
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS
Volume
69
Start Page
1127
End Page
1130
URI
http://scholarworks.bwise.kr/ssu/handle/2018.sw.ssu/11153
DOI
10.1107/S1744309113023877
ISSN
1744-3091
Abstract
Bacteroides thetaiotaomicron BT0793, a putative xylose isomerase, was overexpressed in Escherichia coli, purified and crystallized using polyethylene glycol monomethyl ether 550 as the precipitant. X-ray diffraction data were collected to 2.10 angstrom resolution at 100 Kusing synchrotron X-rays. The crystal was found to belong to space group P1, with unit-cell parameters a = 96.3, b = 101.7, c = 108.3 angstrom, alpha = 82.8, beta = 68.2, gamma = 83.0 degrees. The asymmetric unit contained eight subunits of xylose isomerase with a crystal volume per protein weight (V-M) of 2.38 angstrom(3) Da(-1) and a solvent content of 48.3%.
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College of Natural Sciences (Department of Bioinformatics & Life Science)
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