Crystallization and preliminary X-ray diffraction studies of a protein disulfide oxidoreductase from Aeropyrum pernix K1
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Updated: May 21, 2026

Production, Crystallization and Structure Determination of C. difficile PPEP-1 via Microseeding and Zinc-SAD
Published on: December 30, 2016
Katia D'Ambrosio1, Giuseppina De Simone, Emilia Pedone
1Dipartimento di Chimica Biologica-Sezione Biostrutture, Istituto di Biostrutture e Bioimmagini-CNR, University of Naples Federico II, Via Mezzocannone 16, 80134 Naples, Italy.
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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