title: Crystallization and preliminary crystallographic analysis of mouse peroxiredoxin II with significant pseudosymmetry.
abstract: 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.
authors.affiliation: Institute of Biotechnology, PO Box 65, 00014 University of Helsinki, Finland.
authors.forename: Ari
authors.initials: A
authors.lastname: Ora
authors.forename: Esko
authors.initials: E
authors.lastname: Oksanen
authors.forename: Tommi
authors.initials: T
authors.lastname: Kajander
authors.forename: Adrian
authors.initials: A
authors.lastname: Goldman
authors.forename: Sarah J
authors.initials: SJ
authors.lastname: Butcher
mesh_terms: D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray; D051379:Mice; D054464:Peroxiredoxins / Q000737:chemistry* / Q000378:metabolism; D055503:Protein Multimerization
chemical_list: D054464:Peroxiredoxins