Crystallization of a high potential iron-sulfur protein from the halophilic phototrophic bacterium Ectothiorhodospira halophila.
Crystals of the high-potential iron-sulfur protein from Ectothiorhodospira halophila strain BN 9626 have been grown from 3.4 to 3.5 M ammonium sulfate solutions at pH 7.5. The crystals belong to the space group P21 with unit cell dimensions of a = 60.00 A, b = 31.94 A, c = 40.27 A, and beta = 100.5 degrees. There are 2 molecules/asymmetric unit. The crystals diffract to at least 1.8 A, are stable in the x-ray beam, and are suitable for a high resolution x-ray crystallographic analysis.
D002841:Chromatiaceae / Q000378:metabolism*; D003460:Crystallization; D007506:Iron-Sulfur Proteins / Q000302:isolation & purification; D008667:Metalloproteins / Q000302:isolation & purification; D011487:Protein Conformation; D014961:X-Ray Diffraction
D007506:Iron-Sulfur Proteins; D008667:Metalloproteins