Abstract
Treatment of the 30‐S ribosomal particles by 2.15 M LiCl in the presence of 5 mM MgCl2 results in ribonucleoprotein particles which have a sedimentation coefficient of 25.5 S, are capable of being reconstituted to native 30‐S subparticles, and contain 40–50% of the protein bulk of 30‐S subparticles. A comparison of hydrodynamic and X‐ray data for 30‐S and 25‐S ribonucleoprotein particles suggests that the 25‐S ribonucleoprotein particle retains on the whole the structure of the original 30‐S subparticles and therefore the absent proteins (S1, S2, S3, S5, S9, S10, S12, S14, S20, S21 and possibly S11 and S13) do not take part in maintaining the compact structure of the small subparticle of Escherichia coli ribosomes.
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