Characterization of crystals of tetrameric manganese superoxide dismutase from Thermus thermophilus HB8.
The tetrameric manganese superoxide dismutase from the extreme thermophile Thermus thermophilus HB8 crystallizes in space group P41212 (or its enantiomorph) with a = b = 147.5 A, c = 55.9 A. The diffraction patterns extent to 1.4 A, and the crystals are very resistant to decay induced by x-irradiation. Measurements of the crystal density in Ficoll gradients are consistent with an asymmetric unit containing the entire tetramer (Mr = 80,000).
D008345:Manganese / Q000032:analysis*; D011485:Protein Binding; D011487:Protein Conformation; D013482:Superoxide Dismutase; D013824:Thermus / Q000201:enzymology*; D014961:X-Ray Diffraction
D008345:Manganese; D013482:Superoxide Dismutase