Crystallization and preliminary X-ray diffraction studies of the eukaryotic iron superoxide dismutase (FeSOD) from Vigna unguiculata.
Eukaryotic iron superoxide dismutases (FeSODs) are homodimeric proteins that constitute a fundamental protection against free radicals, which can damage essential cellular mechanisms. The protein was cloned and overexpressed in Escherichia coli with an N-terminal His tag. Crystallization experiments of the protein resulted, after several refined screenings, in crystals suitable for X-ray diffraction analysis. The crystals belong to the monoclinic space group C2, with unit-cell parameters a = 82.54, b = 48.41, c = 64.28 A, alpha = gamma = 90, beta = 119.66 degrees, and contain one molecule per asymmetric unit. At cryogenic temperatures, the crystals diffracted to a resolution limit of 1.80 A using synchrotron radiation at the European Synchrotron Radiation Facility (ESRF).
Muñoz
Inés G
IG
Structural Biology and Biocomputing Programme, Spanish National Cancer Center (CNIO) Macromolecular Crystallography Group, c/Melchor Fdez. Almagro, 3 28029 Madrid, Spain.
Moran
José Fernando
JF
Becana
Manuel
M
Montoya
Guillermo
G
D003460:Crystallization; D018076:DNA, Complementary / Q000096:biosynthesis / Q000235:genetics; D004926:Escherichia coli / Q000378:metabolism; D018532:Pisum sativum / Q000737:chemistry*; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000302:isolation & purification; D013482:Superoxide Dismutase / Q000096:biosynthesis / Q000737:chemistry* / Q000302:isolation & purification; D014961:X-Ray Diffraction
D018076:DNA, Complementary; D011994:Recombinant Proteins; D013482:Superoxide Dismutase