Professor Ada Yonath

Professor Ada Yonath is an Israeli crystallographer best known for her pioneering work on the structure of ribosomes. She is the current Director of the Helen and Milton A. Kimmelman Center for Biomolecular Structure and Assembly of the Weizmann Institute of Science.

In 2009, Yonath received the Nobel Prize in Chemistry along with Venkatraman Ramakrishnan and Thomas A. Steitz for her studies on the structure and function of the ribosome, becoming the first Israeli woman to win the Nobel Prize out of ten Israeli Nobel laureates,[2] the first woman from the Middle East to win a Nobel prize in the sciences and the first woman in 45 years to win the Nobel Prize for Chemistry.

Yonath accepted postdoctoral positions at Carnegie Mellon University (1969) and MIT (1970). While a postdoc at MIT she spent some time in the lab of subsequent 1976 chemistry Nobel Prize winner William N. Lipscomb, Jr. of Harvard University where she was inspired to pursue very large structures.

In 1970, she established what was for nearly a decade the only protein crystallography laboratory in Israel. Then, from 1979 to 1984 she was a group leader with Heinz-Günter Wittmann at the Max Planck Institute for Molecular Genetics in Berlin. She was visiting professor at the University of Chicago in 1977–78. She headed a Max-Planck Institute Research Unit at DESY in Hamburg, Germany (1986–2004) in parallel to her research activities at the Weizmann Institute.

Yonath focuses on the mechanisms underlying protein biosynthesis, by ribosomal crystallography, a research line she pioneered over twenty years ago despite considerable skepticism of the international scientific community. Ribosomes translate RNA into protein and because they have slightly different structures in microbes, when compared to eukaryotes, such as human cells, they are often a target for antibiotics. In 2000 and 2001, she determined the complete high-resolution structures of both ribosomal subunits and discovered within the otherwise asymmetric ribosome, the universal symmetrical region that provides the framework and navigates the process of polypeptide polymerization. Consequently, she showed that the ribosome is a ribozyme that places its substrates in stereochemistry suitable for peptide bond formation and for substrate-mediated catalysis. In 1993 she visualized the path taken by the nascent proteins, namely the ribosomal tunnel, and recently revealed the dynamics elements enabling its involvement in elongation arrest, gating, intra-cellular regulation and nascent chain trafficking into their folding space.

Additionally, Yonath elucidated the modes of action of over twenty different antibiotics targeting the ribosome, illuminated mechanisms of drug resistance and synergism, deciphered the structural basis for antibiotic selectivity and showed how it plays a key role in clinical usefulness and therapeutic effectiveness, thus paving the way for structure-based drug design.

For enabling ribosomal crystallography Yonath introduced a novel technique, cryo bio-crystallography, which became routine in structural biology and allowed intricate projects otherwise considered formidable.

At the Weizmann Institute, Yonath is the incumbent of the Martin S. and Helen Kimmel Professorial Chair. Yonath is a member of the United States National Academy of Sciences; the American Academy of Arts and Sciences; the Israel Academy of Sciences and Humanities; the European Academy of Sciences and Art and the European Molecular Biology Organization. On Saturday, 18 October 2014, Professor Yonath was named an ordinary member of the Pontifical Academy of Sciences by Pope Francis