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Preliminary X-ray crystallographic study of glucose dehydrogenase from Thermus thermophilus HB8

Journal Article · · Acta Crystallographica. Section F
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  1. Bioinformatics Centre (Centre of Excellence in Structural Biology and Biocomputing), Indian Institute of Science, Bangalore 560 012 (India)
  2. RIKEN SPring-8 Center, Harima Institute, 1-1-1 Kouto, Sayo, Hyogo 679-5148 (Japan)
  3. Japan Synchrotron Radiation Research Institute, 1-1-1 Kouto, Sayo, Hyogo 679-5198, Hyogo (Japan)

The glucose dehydrogenase (GDH) protein from T. thermophilus HB8 was cloned, expressed, purified and crystallized. GDH crystals belong to space group P2{sub 1} and diffract to 1.9 Å resolution. Thermus thermophilus is an aerobic chemoorganotroph that has been found to grow anaerobically in the presence of nitrate. Crystals of glucose dehydrogenase (GDH) from T. thermophilus HB8 belong to space group P2{sub 1}, with unit-cell parameters a = 36.90, b = 132.96, c = 60.78 Å, β = 97.2°. Preliminary studies and molecular-replacement calculations reveal that the asymmetric unit contains two monomers.

OSTI ID:
22360320
Journal Information:
Acta Crystallographica. Section F, Journal Name: Acta Crystallographica. Section F Journal Issue: Pt 5 Vol. 63; ISSN ACSFCL; ISSN 1744-3091
Country of Publication:
United Kingdom
Language:
English

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