Figure 1. Constituents of the E. coli ribosome, according to Wittmann HG (1976) The Seventh Sir Hans Krebs Lecture: Structure, Function and Evolution of Ribosomes. European Journal of Biochemistry 61: 1–13.

Figure 2. Two-dimensional gel electrophoresis pattern of the total 70S ribosomal protein mixture derived from the ribosome of E. coli (MRE 600), separated by differences in charge and molecular mass, according to Kaltschmidt E and Wittmann HG (1970) Ribsomal proteins XII. Number of proteins in small and large ribosomal subunits of Escherichia coli as determined by two-dimensional gel electrophoresis. Proceedings of the National Academy of Sciences of the USA 67: 93–106.

Figure 3. Secondary structure of the 16S RNA (the 5¢-part is shown) derived from E. coli, according to Brimacombe R, Greuer B, Mitchell P, Osswald M, Rinke-Appel J, Schueler D and Stade K (1990) Three-dimensional structure and function of Escherichia coli 16S and 23S rRNA as studied by cross-linking techniques. In: Hill WE et al. (eds) The Ribosome, Structure, Function and Evolution, pp. 93–106. Washington DC: American Society for Microbiology.

Figure 4. Topography of r-proteins within E. coli ribosomes as obtained by electron microscopy of anti-r-protein antibodies bound to 30S and 50S subunits, according to Stöffler G and Stöffler-Meilicke M (1990) Topography of the ribosomal proteins from Escherichia coli within the intact subunits as determined by immunoelectron microscopy and protein–protein cross-linking. In: Hill WE et al. (eds) The Ribosome, Structure, Function and Evolution, pp. 123–133. Washington DC: American Society for Microbiology. The numbers indicate the location of the r-proteins of the 30S subunit (upper row) and of the 50S subunit (lower row).

Figure 5. Total reconstitution of the ribosome from the constituents, as exemplified with the 50S subunit of E. coli ribosomes, according to Dohme F and Nierhaus KH (1976) Total reconstruction and assembly of 50S subunits from Escherichia coli in vitro. Journal of Molecular Biology 107: 585–599.

Figure 6. Topography of r-proteins (black balls) and the various helix regions of the 16S RNA within the E. coli 30S subunit as obtained by neutron scattering and fitted to a cryoelectron microscopic model of the ribosome at a resolution of 20 Å, according to Brimacombe R, Greuer B, Mitchell P, Osswald M, Rinke-Appel J, Schueler D and Stade K (1990) Three-dimensional structure and function of Escherichia coli 16S and 23S rRNA as studied by cross-linking techniques. In: Hill WE et al. (eds) The Ribosome, Structure, Function and Evolution, pp. 93–106. Washington DC: American Society for Microbiology. (See also Stark H, Orlova EV, Rinke-Appel J et al. (1997) Arrangement of tRNAs in pre- and posttranslocational ribosomes revealed by electron cryomicroscopy. Cell 88: 19–28.

Figure 7. Contact sites between the rRNA and the binding proteins established at the molecular level by crosslinking experiments.

Figure 8. Three-dimensional model of the ribosome as derived from cryoelectromicroscopy, according to Frank J, Zhu J, Penczek P et al. (1995) A model of protein synthesis based on cryo-electron microscopy of the E. coli ribosome. Nature 376: 441–444.

Figure 9. Comparison of the gene operon S10 in E. coli, and the archaeal organisms Halobacterium marismortui and Methanococcus vannielii. The same colour is used to indicate the same protein genes in the three different organisms.