title: Crystallization and preliminary X-ray diffraction studies of a protein disulfide oxidoreductase from Aeropyrum pernix K1.
abstract: A protein disulfide oxidoreductase from the archaeon Aeropyrum pernix K1 has been overexpressed in Escherichia coli and crystallized at 298 K using the hanging-drop vapour-diffusion method. Crystals belong to the space group I222 or I2(1)2(1)2(1), with unit-cell parameters a = 90.59, b = 102.43, c = 128.96 A. A complete data set has been collected at the Elettra synchrotron source in Trieste to 1.93 A resolution using a single frozen crystal.
authors.affiliation: Dipartimento di Chimica Biologica-Sezione Biostrutture, 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: D041522:Aeropyrum / Q000201:enzymology*; D019843:Archaeal Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification; D003001:Cloning, Molecular; D003460:Crystallization; D004926:Escherichia coli / Q000201:enzymology; D050862:Oxidoreductases Acting on Sulfur Group Donors / Q000737:chemistry* / Q000302:isolation & purification; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification; D014961:X-Ray Diffraction
chemical_list: D019843:Archaeal Proteins; D011994:Recombinant Proteins; D050862:Oxidoreductases Acting on Sulfur Group Donors