Open AccessCrystallization and preliminary crystallographic analysis of mouse peroxiredoxin II with significant pseudosymmetry
Author(s) -
Ora Ari,
Oksanen Esko,
Kajander Tommi,
Goldman Adrian,
Butcher Sarah J.
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110003684
Subject(s) - crystallization , crystallography , peroxiredoxin , protein crystallization , chemistry , crystal (programming language) , escherichia coli , recombinant dna , resolution (logic) , solvent , biochemistry , enzyme , artificial intelligence , peroxidase , programming language , organic chemistry , computer science , gene
Peroxiredoxin II was cloned from mouse B cells into pCold 1 expression vector and produced as a His‐tagged recombinant protein in Escherichia coli . A ring form was isolated by gel filtration. A crystal obtained by the sitting‐drop vapour‐diffusion method diffracted to 1.77 Å resolution at 100 K. The crystal belonged to space group P 2 1 2 1 2, with unit‐cell parameters a = 117.4, b = 133.9, c = 139.1 Å. The asymmetric unit is expected to contain six dimers of peroxiredoxin II, with a corresponding solvent content of 39.3%. Peaks in the native Patterson function together with pseudo‐systematic absences suggested that the crystals suffered from severe translational pseudosymmetry.