Expression, purification and X-ray analysis of 1,3-propanediol dehydrogenase (Aq_1145) from Aquifex aeolicus VF5
Data(s) |
01/02/2010
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Resumo |
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 angstrom. The crystal belonged to space group P3(2), with unit-cell parameters a = b = 142.19, c = 123.34 angstrom. The structure contained two dimers in the asymmetric unit and was solved by the MR-SAD approach. |
Formato |
application/pdf |
Identificador |
http://eprints.iisc.ernet.in/25822/1/nj5048.pdf Jeyakanthan, Jeyaraman and Thamotharan, Subbiah and Panjikar, Santosh and Kitamura, Yoshiaki and Nakagawa, Noriko and Shinkai, Akeo and Kuramitsu, Seiki and Yokoyama, Shigeyuki (2010) Expression, purification and X-ray analysis of 1,3-propanediol dehydrogenase (Aq_1145) from Aquifex aeolicus VF5. In: Acta Crystallographica Section F, 66 (Part 2). pp. 184-186. |
Publicador |
John Wiley and Sons |
Relação |
http://scripts.iucr.org/cgi-bin/paper?S1744309109052403 http://eprints.iisc.ernet.in/25822/ |
Palavras-Chave | #Molecular Biophysics Unit |
Tipo |
Journal Article PeerReviewed |