Expression, purification and X-ray analysis of 1,3 - Propanediol dehydrogenase (Aq-1145) from Aquifex aeolicus VF5

Jeyaraman Jeyakanthan, Subbiah Thamotharan, Santosh Panjikar, Yoshiaki Kitamura, Noriko Nakagawa, Akeo Shinkai, Seiki Kuramitsu, Shigeyuki Yokoyama

Research output: Contribution to journalArticleResearchpeer-review

3 Citations (Scopus)


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 Å. The crystal belonged to space group P32, with unit-cell parameters a = b = 142.19, c = 123.34 Å. The structure contained two dimers in the asymmetric unit and was solved by the MR-SAD approach.

Original languageEnglish
Pages (from-to)184-186
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Issue number2
Publication statusPublished - 2010
Externally publishedYes

Cite this