Crystallization and preliminary crystallographic analysis of mouse peroxiredoxin II with significant pseudosymmetry.
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 A resolution at 100 K. The crystal belonged to space group P2(1)2(1)2, with unit-cell parameters a = 117.4, b = 133.9, c = 139.1 A. 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.
Ora
Ari
A
Institute of Biotechnology, PO Box 65, 00014 University of Helsinki, Finland.
Oksanen
Esko
E
Kajander
Tommi
T
Goldman
Adrian
A
Butcher
Sarah J
SJ
D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray; D051379:Mice; D054464:Peroxiredoxins / Q000737:chemistry* / Q000378:metabolism; D055503:Protein Multimerization
D054464:Peroxiredoxins