Architecture of the E.coli 70S ribosome

N. Burkhardt; G. Diedrich; K.H. Nierhaus; W. Meerwinck; H.B. Stuhrmann; J.S. Pedersen; M.H.J. Koch; V.V. Volkov; M.B. Kozin; D.I. Svergun

doi:10.1016/S0921-4526(96)00910-6

Architecture of the E.coli 70S ribosome

N. Burkhardt, G. Diedrich, K.H. Nierhaus, W. Meerwinck, H.B. Stuhrmann, J.S. Pedersen, M.H.J. Koch, V.V. Volkov, M.B. Kozin, D.I. Svergun

Research output: Contribution to journal › Journal article › Research

Abstract

The 70S ribosome from E.coli was analysed by neutron scattering focusing on the shape and the internal protein-RNA-distribution of the complex. Measurements on selectively deuterated 70S particles and free 30S and 50S subunits applying conventional contrast variation and proton-spin contrast-variation resulted in a total of 42 scattering curves. Processing the data on the basis of the spherical harmonic technique, a four-phase model for the 70S ribosome could be generated, which describes the shape of the particle as well as the protein- and the RNA-moieties of each subunit at about 35 Angstrom resolution.

Original language	English
Journal	Physica B: Condensed Matter
Volume	234/236
Pages (from-to)	199-201
ISSN	0921-4526
DOIs	https://doi.org/10.1016/S0921-4526(96)00910-6
Publication status	Published - 1997

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title = "Architecture of the E.coli 70S ribosome",

abstract = "The 70S ribosome from E.coli was analysed by neutron scattering focusing on the shape and the internal protein-RNA-distribution of the complex. Measurements on selectively deuterated 70S particles and free 30S and 50S subunits applying conventional contrast variation and proton-spin contrast-variation resulted in a total of 42 scattering curves. Processing the data on the basis of the spherical harmonic technique, a four-phase model for the 70S ribosome could be generated, which describes the shape of the particle as well as the protein- and the RNA-moieties of each subunit at about 35 Angstrom resolution. ",

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author = "N. Burkhardt and G. Diedrich and K.H. Nierhaus and W. Meerwinck and H.B. Stuhrmann and J.S. Pedersen and M.H.J. Koch and V.V. Volkov and M.B. Kozin and D.I. Svergun",

year = "1997",

doi = "10.1016/S0921-4526(96)00910-6",

language = "English",

volume = "234/236",

pages = "199--201",

journal = "Physica B: Condensed Matter",

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TY - JOUR

T1 - Architecture of the E.coli 70S ribosome

AU - Burkhardt, N.

AU - Diedrich, G.

AU - Nierhaus, K.H.

AU - Meerwinck, W.

AU - Stuhrmann, H.B.

AU - Pedersen, J.S.

AU - Koch, M.H.J.

AU - Volkov, V.V.

AU - Kozin, M.B.

AU - Svergun, D.I.

PY - 1997

Y1 - 1997

N2 - The 70S ribosome from E.coli was analysed by neutron scattering focusing on the shape and the internal protein-RNA-distribution of the complex. Measurements on selectively deuterated 70S particles and free 30S and 50S subunits applying conventional contrast variation and proton-spin contrast-variation resulted in a total of 42 scattering curves. Processing the data on the basis of the spherical harmonic technique, a four-phase model for the 70S ribosome could be generated, which describes the shape of the particle as well as the protein- and the RNA-moieties of each subunit at about 35 Angstrom resolution.

AB - The 70S ribosome from E.coli was analysed by neutron scattering focusing on the shape and the internal protein-RNA-distribution of the complex. Measurements on selectively deuterated 70S particles and free 30S and 50S subunits applying conventional contrast variation and proton-spin contrast-variation resulted in a total of 42 scattering curves. Processing the data on the basis of the spherical harmonic technique, a four-phase model for the 70S ribosome could be generated, which describes the shape of the particle as well as the protein- and the RNA-moieties of each subunit at about 35 Angstrom resolution.

KW - Nye funktionelle materialer

U2 - 10.1016/S0921-4526(96)00910-6

DO - 10.1016/S0921-4526(96)00910-6

M3 - Journal article

VL - 234/236

SP - 199

EP - 201

JO - Physica B: Condensed Matter

JF - Physica B: Condensed Matter

SN - 0921-4526

ER -

Architecture of the E.coli 70S ribosome

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