Crystallization and preliminary X-ray diffraction studies of a protein disulfide oxidoreductase from Aquifex aeolicus.
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%.
D'Ambrosio
Katia
K
Dipartimento di Chimica Biologica-Sezione Biostrutture and 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
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
D001426:Bacterial Proteins; D009247:NADH, NADPH Oxidoreductases