Open AccessCrystallization and preliminary X‐ray diffraction studies of a protein disulfide oxidoreductase from Aeropyrum pernix K1
Author(s) -
D'Ambrosio Katia,
De Simone Giuseppina,
Pedone Emilia,
Rossi Mosè,
Bartolucci Simonetta,
Pedone Carlo
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309105004057
Subject(s) - crystallization , crystallography , x ray crystallography , oxidoreductase , x ray , diffraction , disulfide bond , materials science , chemistry , biochemistry , physics , enzyme , organic chemistry , optics
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 I 222 or I 2 1 2 1 2 1 , with unit‐cell parameters a = 90.59, b = 102.43, c = 128.96 Å. A complete data set has been collected at the Elettra synchrotron source in Trieste to 1.93 Å resolution using a single frozen crystal.
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