Molecular symmetry of Lumbricus erythrocruorin.
X-ray diffraction data to a minimum Bragg spacing of 5.5 A have been collected from crystals of Lumbricus terrestris erthrocruorin, a 3.9 x 10(6)-dalton respiratory protein. Self-rotation function calculations from these data reveal D6 symmetry to a resolution of at least 6 A. These calculations show that erythrocruorin molecules pack in their crystals with molecular diads coincident with crystallographic diads along the a axis. Packing constraints limit the position of the molecular center to within 40 A of x = 1/4a.
Royer
W E
WE
Howard Hughes Medical Institute, Department of Biochemistry and Molecular Biophysics, Columbia University, New York, New York 10032.
Hendrickson
W A
WA
D000818:Animals; D000845:Annelida / Q000032:analysis*; D055598:Chemical Phenomena; D002621:Chemistry; D003460:Crystallization; D004902:Erythrocruorins; D006454:Hemoglobins
D004902:Erythrocruorins; D006454:Hemoglobins