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  • Title: Shape of protein L11 from the 50S ribosomal subunit of Escherichia coli.
    Author: Giri L, Dijk J, Labischinski H, Bradaczek H.
    Journal: Biochemistry; 1978 Feb 21; 17(4):745-9. PubMed ID: 341976.
    Abstract:
    Protein L11 from the 50S ribosomal subunit of Escherichia coli A19 was purified by a method using nondenaturing conditions. Its shape in solution was studied by hydrodynamic and low-angle x-ray scattering experiments. The results from both methods are in good agreement. In buffers similar to the ribosomal reconstitution buffer, the protein is monomeric at concentrations up to 3 mg/mL and has a molecular weight of 16 000-17 000. The protein molecule resembles a prolate ellipsoid with an axial ratio of 5-6:1 a radius of gyration of 34 A, and a maximal length of 150 A. From the low-angle x-ray diffraction data, a more refined model of the protein molecule has been constructed consisting of two ellipsoids joined by their long axes.
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