PMID:7880961
| Citation |
Igarashi, Y, Kimura, K, Ichimura, K, Matsuzaki, S, Ikura, T, Kuwajima, K and Kihara, H (1995) Solution X-ray scattering study on the chaperonin GroEL from Escherichia coli. Biophys. Chem. 53:259-66 |
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| 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. |
| Links | |
| Keywords |
Chaperonin 60/chemistry; Escherichia coli/chemistry; Models, Chemical; Protein Conformation; Scattering, Radiation; Solutions; X-Rays |
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