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Related Experiment Videos

An x-ray diffraction study of ribosome structure.

A D Dolgov, D A Ivanov, K A Kapitonova

    Molecular Biology
    |January 1, 1975
    PubMed
    Summary
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    X-ray diffraction reveals that the 50 S ribosomal subunit of E. coli has a periodic internal structure. This periodicity is dependent on water content and ionic strength, and is reversible.

    Area of Science:

    • Structural Biology
    • Biophysics
    • Molecular Biology

    Background:

    • Ribosomes are complex molecular machines responsible for protein synthesis.
    • Understanding the internal structure of ribosomal subunits is crucial for elucidating their function.
    • Previous studies have explored ribosomal structure, but detailed internal periodicity remains an area of investigation.

    Purpose of the Study:

    • To investigate the internal structure and organization of E. coli 70 S ribosomes and their subunits using X-ray diffraction.
    • To determine the influence of water content and ionic strength on the structural integrity and periodicity of ribosomal particles.
    • To compare the structural properties of intact ribosomes, subunits, and related ribonucleoprotein (RNP) particles.

    Main Methods:

    Related Experiment Videos

  • X-ray diffraction analysis of dense gels of E. coli 70 S ribosomes, 50 S subunits, CM-like particles, RNP strands, and free rRNA.
  • Comparison of experimental X-ray scattering data with diffraction curves calculated for various model ellipsoidal structures.
  • Investigation of structural changes under varying conditions of salt concentration and water content.

    • Main Results:

    • The 50 S ribosomal subunit exhibits a periodic internal structure, forming a lattice with spacings of approximately 42 and 28 Å at a water content of 0.8 g/g.
    • This periodic structure is disrupted when the water content drops below 0.2 g/g, but this disruption is reversible.
    • CM-like particles show similar internal periodicity to 50 S subunits at high ionic strength (2 M LiCl) but lose this periodicity at low ionic strength.

    Conclusions:

    • The internal structure of the E. coli 50 S ribosomal subunit is periodic, suggesting a well-defined arrangement of its components.
    • Ribosomal structure and periodicity are sensitive to water content and ionic strength, with reversible changes observed.
    • The findings provide insights into the structural organization of ribosomal particles and their stability under different environmental conditions.