Crystallization and preliminary X-ray diffraction studies of a protein disulfide oxidoreductase from Aeropyrum pernix K1.
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.
D'Ambrosio
Katia
K
Dipartimento di Chimica Biologica-Sezione Biostrutture, Istituto di Biostrutture e Bioimmagini-CNR, University of Naples Federico II, Via Mezzocannone 16, 80134 Naples, Italy.
De Simone
Giuseppina
G
Pedone
Emilia
E
Rossi
Mosè
M
Bartolucci
Simonetta
S
Pedone
Carlo
C
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
D019843:Archaeal Proteins; D011994:Recombinant Proteins; D050862:Oxidoreductases Acting on Sulfur Group Donors