Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Solution scattering from 50S ribosomal subunit resolves inconsistency between electron microscopic models

D I Svergun1, J S Pedersen, I N Serdyuk

  • 1European Molecular Biology Laboratory, Deutsches Elektronen Synchrotron, Hamburg, Germany.

Proceedings of the National Academy of Sciences of the United States of America
|December 6, 1994
PubMed
Summary

Electron microscopy models of the 50S ribosomal subunit differ. This study reveals the native Escherichia coli 50S subunit shape and its RNA-rich core using scattering data, showing electron microscopy models are biased toward RNA.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

NOD1 mediates interleukin-18 processing in epithelial cells responding to Helicobacter pylori infection in mice.

Nature communications·2023
Same author

Diffusion Coefficients of the 45S and 50S States of the Large Ribosomal Subunit of E. coli by Quasielastic Light Scattering.

Journal of research of the National Bureau of Standards (1977)·2021
Same author

Correction for Shtykova et al., "Solution Structure, Self-Assembly, and Membrane Interactions of the Matrix Protein from Newcastle Disease Virus at Neutral and Acidic pH".

Journal of virology·2021
Same author

ASAXS measurements on ferritin and apoferritin at the bioSAXS beamline P12 (PETRA III, DESY).

Journal of applied crystallography·2021
Same author

MPBuilder: A PyMOL Plugin for Building and Refinement of Solubilized Membrane Proteins Against Small Angle X-ray Scattering Data.

Journal of molecular biology·2021
Same author

A THz transparent 3D printed microfluidic cell for small angle x-ray scattering.

The Review of scientific instruments·2020

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biophysics

Background:

  • Models of the 50S ribosomal subunit derived from electron microscopy (EM) of isolated particles and ordered sheets present discrepancies.
  • Understanding the accurate three-dimensional structure of the 50S ribosomal subunit is crucial for deciphering protein synthesis mechanisms.

Purpose of the Study:

  • To generate a high-resolution model of the native 50S ribosomal subunit from Escherichia coli in solution.
  • To characterize the structure of the RNA-rich core of the 50S subunit.
  • To compare structural models derived from different experimental techniques.

Main Methods:

  • Joint interpretation of X-ray and neutron small-angle scattering (SAS) data.
  • Contrast variation techniques were employed to differentiate between RNA and protein components.

Related Experiment Videos

  • A 4-nm resolution model was generated using the combined SAS data.

    • Main Results:

    • A model of the native 50S ribosomal subunit shape in solution was successfully generated at 4-nm resolution.
    • A distinct model of the RNA-rich core was also resolved.
    • The SAS-derived model of the entire subunit showed good agreement with EM models of isolated particles.
    • The SAS-derived model of the RNA-rich core aligned well with EM models from ordered sheets.

    Conclusions:

    • The 50S ribosomal subunit model derived from ordered sheets in EM studies appears to be significantly biased towards the RNA component.
    • The native structure of the 50S ribosomal subunit in solution, as determined by combined X-ray and neutron SAS, provides a more accurate representation.
    • Discrepancies in EM models highlight the importance of using complementary techniques for structural determination.