Crystallization and preliminary X-ray data of a bifunctional peroxiredoxin from poplar

Two variants (wild type and V152C mutant) of a bifunctional poplar peroxiredoxin have been overexpressed in Escherichia coli cells. The two recombinant enzymes were purified and crystallized using the hanging-drop vapour-diffusion technique. Data sets were collected to 1.62 and 2.48 Å resolution using X-ray synchrotron-source radiation from two crystal forms of wild-type peroxiredoxin which belonged to the monoclinic space group P2₁ (with unit-cell parameters a = 59.26, b = 68.80, c = 75.71 Å, β = 93.45°) and to the orthorhombic space group P2₁2₁2 (with unit-cell parameters a = 64.70, b = 130.73, c = 35.59 Å), respectively. Data were also collected to 2.17 Å resolution using a home X-ray source from a V152C peroxiredoxin crystal which belongs to the triclinic space group (P1), with unit-cell parameters a = 36.65, b = 41.53, c = 58.06 Å, α = 70.52, β = 93.45, γ = 64.31°. Phases have been obtained using molecular replacement with the structure of human peroxiredoxin V (PDB code 1hd2) as a search model. Refinement of the structures is in progress.