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The measurement of the locations and radii of gyration of proteins in the 30S ribosomal subunit of E. coli by neutron scattering
Author(s) -
Moore P. B.,
Langer J. A.,
Engelman D. M.
Publication year - 1978
Publication title -
journal of applied crystallography
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.429
H-Index - 162
ISSN - 1600-5767
DOI - 10.1107/s0021889878013643
Subject(s) - gyration , ribosome , radius of gyration , neutron scattering , neutron , 30s , physics , scattering , small angle neutron scattering , ribosomal protein , protein subunit , ribosomal rna , small angle scattering , crystallography , chemistry , nuclear physics , optics , nuclear magnetic resonance , polymer , rna , mathematics , geometry , biochemistry , gene
The theory of the technique currently in use for measuring distances between subunits in macromolecular aggregates by neutron small‐angle scattering is outlined. It is shown that estimates for the radii of gyration of subunits within aggregates can be extracted from neutron distance data, in addition to the distances themselves. The current status of efforts to apply these methods to determine the structure of the E. coli ribosome is discussed.