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  • Title: Crystallization and preliminary X-ray diffraction studies of a protein disulfide oxidoreductase from Aeropyrum pernix K1.
    Author: D'Ambrosio K, De Simone G, Pedone E, Rossi M, Bartolucci S, Pedone C.
    Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun; 2005 Mar 01; 61(Pt 3):335-6. PubMed ID: 16511034.
    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.
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