We have obtained many insights into the structural basis of ribosome function in protein synthesis from our structural studies of the large ribosomal subunit as well as the 70S bacterial ribosome, and their complexes with substrates, protein factors or antibiotics.  These have elucidated the mechanism by which this ribozyme catalyzes peptide bond formation as well as the specificity and mode of its inhibition by antibiotics.

 During the process of protein synthesis elongation, the 70S ribosome is in various conformational states bound to various protein factors that play critical roles in protein synthesis.  We have now determined the structures of several of these functional states. 

 The structures of some of our antibiotic complexes have been used by Rib-X Pharmaceuticals, Inc. to develop new compounds that are effective against MRSA, one of which has successfully completed phase II clinical trials.  Recently, we have determined the crystal structures of the 70S ribosome bound to two compounds that are effective against tuberculosis, capreomycin and viomycin; the design of new anti-TB antibiotics may be possible by chemically combining components of these compounds with neighboring compounds.