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 A resolution using X-ray synchrotron-source radiation from two crystal forms of wild-type peroxiredoxin which belonged to the monoclinic space group P2(1) (with unit-cell parameters a = 59.26, b = 68.80, c = 75.71 A, beta = 93.45 degrees ) and to the orthorhombic space group P2(1)2(1)2 (with unit-cell parameters a = 64.70, b = 130.73, c = 35.59 A), respectively. Data were also collected to 2.17 A 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 A, alpha = 70.52, beta = 93.45, gamma = 64.31 degrees. 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.
Echalier
Aude
A
LCM3B, Groupe Biocristallographie, UMR 7036, UHP, Faculté des Sciences, 54506 Vandoeuvre CEDEX, France.
Corbier
Catherine
C
Rouhier
Nicolas
N
Jacquot
Jean Pierre
JP
Aubry
André
A
D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D010544:Peroxidases / Q000737:chemistry* / Q000235:genetics; D054464:Peroxiredoxins; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D014197:Trees / Q000201:enzymology*
D011994:Recombinant Proteins; D010544:Peroxidases; D054464:Peroxiredoxins