Structural highlights
Publication Abstract from PubMed
An NAD(+)-dependent psychrophilic alcohol dehydrogenase (ADH) from the Antarctic psychrophile Moraxella sp. TAE123 has been purified to homogeneity. The enzyme consists of four identical subunits, each containing two Zn ions. Protein crystals suitable for X-ray diffraction were obtained under optimized salting-out crystallization conditions using ammonium sulfate as a precipitating agent. The crystals are hexagonal bipyramids and belong to space group P3(1)21 or P3(2)21, with unit-cell parameters a = 136.4, c = 210.7 A. They contain one protein homotetramer in the asymmetric unit. Diffraction data were collected to 2.2 A under cryogenic conditions using synchrotron radiation.
Crystallization and preliminary X-ray diffraction studies of an alcohol dehydrogenase from the Antarctic psychrophile Moraxella sp. TAE123.,Papanikolau Y, Tsigos I, Papadovasilaki M, Bouriotis V, Petratos K Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Feb 1;61(Pt 2):246-8. Epub, 2005 Feb 1. PMID:16511007[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Papanikolau Y, Tsigos I, Papadovasilaki M, Bouriotis V, Petratos K. Crystallization and preliminary X-ray diffraction studies of an alcohol dehydrogenase from the Antarctic psychrophile Moraxella sp. TAE123. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Feb 1;61(Pt 2):246-8. Epub, 2005 Feb 1. PMID:16511007 doi:http://dx.doi.org/10.1107/S1744309105002253
