Crystallization and preliminary X-ray diffraction study of a protein with a high potential rubredoxin center and a hemerythrin-type Fe center.
A newly discovered iron-containing protein, isolated from the bacterium Desulfovibrio vulgaris (Hildenborough, NCIB 8303), has been crystallized. The molecule appears to be a dimer of mass 44kDa. This protein has iron centers with spectrascopic similarities to those in rubredoxins and in hemerythrins. The X-ray diffraction shows symmetry consistent with space group I222 or I212121. Cell parameters are a = 49.2 A, b = 81.3 A, c = 100.1 A, and alpha, beta, gamma = 90 degrees. X-ray diffraction data have been collected to 3.0 A, and a search for useful heavy atom derivatives is in progress for the analysis of the crystal structure of this Fe-protein.
Sieker
L C
LC
Department of Biological Structure, University of Washington, Seattle 98195.
Turley
S
S
Prickril
B C
BC
LeGall
J
J
D003460:Crystallization; D005288:Ferredoxins / Q000032:analysis*; D006422:Hemerythrin / Q000032:analysis*; D008667:Metalloproteins / Q000032:analysis*; D008970:Molecular Weight; D011506:Proteins / Q000032:analysis*; D012416:Rubredoxins / Q000032:analysis*; D014961:X-Ray Diffraction
D005288:Ferredoxins; D006422:Hemerythrin; D008667:Metalloproteins; D011506:Proteins; D012416:Rubredoxins