| Literature DB >> 20124718 |
Jeyaraman Jeyakanthan1, Subbiah Thamotharan, Santosh Panjikar, Yoshiaki Kitamura, Noriko Nakagawa, Akeo Shinkai, Seiki Kuramitsu, Shigeyuki Yokoyama.
Abstract
1,3-Propanediol dehydrogenase is an enzyme that catalyzes the oxidation of 1,3-propanediol to 3-hydroxypropanal with the simultaneous reduction of NADP(+) to NADPH. SeMet-labelled 1,3-propanediol dehydrogenase protein from the hyperthermophilic bacterium Aquifex aeolicus VF5 was overexpressed in Escherichia coli and purified to homogeneity. Crystals of this protein were grown from an acidic buffer with ammonium sulfate as the precipitant. Single-wavelength data were collected at the selenium peak to a resolution of 2.4 A. The crystal belonged to space group P3(2), with unit-cell parameters a = b = 142.19, c = 123.34 A. The structure contained two dimers in the asymmetric unit and was solved by the MR-SAD approach.Entities:
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Year: 2010 PMID: 20124718 PMCID: PMC2815688 DOI: 10.1107/S1744309109052403
Source DB: PubMed Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun ISSN: 1744-3091