title: Crystallization and preliminary X-ray diffraction studies of a protein disulfide oxidoreductase from Aquifex aeolicus.
abstract: A protein disulfide oxidoreductase from the thermophilic bacterium Aquifex aeolicus has been overexpressed in Escherichia coli and crystallized at 298 K using the hanging-drop vapour-diffusion method. Crystals belong to space group R32, with unit-cell parameters a = b = 161.1, c = 153.1 A. A complete data set has been collected to 2.4 A using synchrotron radiation. Packing-density considerations agree with the presence of 2-4 monomers in the asymmetric unit, with a corresponding solvent content of 66-32%.
authors.affiliation: Dipartimento di Chimica Biologica-Sezione Biostrutture and Istituto di Biostrutture e Bioimmagini-CNR, University of Naples Federico II, via Mezzocannone 16, 80134 Naples, Italy.
authors.forename: Katia
authors.initials: K
authors.lastname: D'Ambrosio
authors.forename: Giuseppina
authors.initials: G
authors.lastname: De Simone
authors.forename: Emilia
authors.initials: E
authors.lastname: Pedone
authors.forename: Mosè
authors.initials: M
authors.lastname: Rossi
authors.forename: Simonetta
authors.initials: S
authors.lastname: Bartolucci
authors.forename: Carlo
authors.initials: C
authors.lastname: Pedone
mesh_terms: D001419:Bacteria / Q000201:enzymology*; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D003460:Crystallization; D018360:Crystallography, X-Ray; D009247:NADH, NADPH Oxidoreductases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification
chemical_list: D001426:Bacterial Proteins; D009247:NADH, NADPH Oxidoreductases