title: Solution X-ray scattering study on the chaperonin GroEL from Escherichia coli.
abstract: The molecular architecture of native GroEL has been studied by solution X-ray scattering. The radius of gyration for the native molecule was estimated to be 66.0 A in 50 mM Tris-HCl, 100 mM KCl at pH 7.5 and 25 degrees C. The maximum dimension was estimated to be 170 A, based on the pair distance distribution function. A cylindrical structure or two heptameric rings was found to be the best for native GroEL among structures examined by using a multi-sphere model analysis in which the radius of constituent sphere was 6 A. The results of the model analysis show that the radius of GroEL is 68.0 A and the height is 150.7 A. Unexpectedly, the central penetrating hole through GroEL was not confirmed in the best-fit structure.
authors.affiliation: Department of Biochemistry, Dokkyo University School of Medicine, Tochigi, Japan.
authors.forename: Y
authors.initials: Y
authors.lastname: Igarashi
authors.forename: K
authors.initials: K
authors.lastname: Kimura
authors.forename: K
authors.initials: K
authors.lastname: Ichimura
authors.forename: S
authors.initials: S
authors.lastname: Matsuzaki
authors.forename: T
authors.initials: T
authors.lastname: Ikura
authors.forename: K
authors.initials: K
authors.lastname: Kuwajima
authors.forename: H
authors.initials: H
authors.lastname: Kihara
mesh_terms: D018834:Chaperonin 60 / Q000737:chemistry*; D004926:Escherichia coli / Q000737:chemistry*; D008956:Models, Chemical; D011487:Protein Conformation; D012542:Scattering, Radiation; D012996:Solutions; D014965:X-Rays
chemical_list: D018834:Chaperonin 60; D012996:Solutions