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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.

SUBMITTER: Ora A

PROVIDER: S-EPMC2833056 | biostudies-literature | 2010 Mar

REPOSITORIES: biostudies-literature

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Crystallization and preliminary crystallographic analysis of mouse peroxiredoxin II with significant pseudosymmetry.

Ora Ari A Oksanen Esko E Kajander Tommi T Goldman Adrian A Butcher Sarah J SJ

Acta crystallographica. Section F, Structural biology and crystallization communications 20100227 Pt 3

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 correspondin ...[more]

PMID: 20208180

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