title: Crystals of Lumbricus erythrocruorin.
abstract: Lumbricus terrestris erythrocruorin, a 3.9 X 10(6) Mr respiratory protein, has been crystallized in four different forms. Despite the high molecular symmetry apparent from images in electron micrographs, only one crystal form expresses any molecular symmetry as crystallographic symmetry. The lattice parameters provide upper limits on the molecular dimensions of 267 A X 308 A X 172 A (1 A = 0.1 nm), which agree well with dimensions obtained from electron micrographs of negatively stained molecules. We have collected diffraction data to 5.5 A from type III crystals and have begun a structural analysis.
authors: Howard Hughes Medical Institute, Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032.
authors: W E
authors: WE
authors: Royer
authors: W A
authors: WA
authors: Hendrickson
authors: W E
authors: WE
authors: Love
mesh_terms: D000818:Animals; D000845:Annelida; D003461:Crystallography; D004902:Erythrocruorins; D006454:Hemoglobins; D014961:X-Ray Diffraction
chemical_list: D004902:Erythrocruorins; D006454:Hemoglobins