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.
Crystallization and preliminary x-ray diffraction studies of a protein disulfide oxidoreductase from Aeropyrum pernix K1 / D'Ambrosio, K.; De Simone, G.; Pedone, E.; Rossi, Mose'; Bartolucci, Simonetta; Pedone, Carlo. - In: ACTA CRYSTALLOGRAPHICA. SECTION F, STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS. - ISSN 1744-3091. - STAMPA. - F61:3(2005), pp. 335-336. [10.1107/S0907444904022632]
Crystallization and preliminary x-ray diffraction studies of a protein disulfide oxidoreductase from Aeropyrum pernix K1
ROSSI, MOSE';BARTOLUCCI, SIMONETTA;PEDONE, CARLO
2005
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.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
