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 Ê . A complete data set has been collected to 2.4 A Ê 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%.
Crystallization and preliminary x-ray diffraction studies of a protein disulfide oxidoreductase from Aquifex aeolicus / D'Ambrosio, K.; De Simone, G.; Pedone, E.; Rossi, Mose'; Bartolucci, Simonetta; Pedone, Carlo. - In: ACTA CRYSTALLOGRAPHICA. - ISSN 0365-110X. - STAMPA. - D60:11(2004), pp. 2076-2077. [10.1107/S0907444904022632]
Crystallization and preliminary x-ray diffraction studies of a protein disulfide oxidoreductase from Aquifex aeolicus
ROSSI, MOSE';BARTOLUCCI, SIMONETTA;PEDONE, CARLO
2004
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 Ê . A complete data set has been collected to 2.4 A Ê 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%.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
