Ada Yonath, at the Weizmann Institute in Israel, begins in the 1970s a line of research the scientific community considered practically unfeasible: determining the complete three-dimensional structure of the ribosome, the huge molecular machine — composed of RNA and dozens of distinct proteins — responsible for synthesizing all of the cell's proteins by translating the information carried by messenger RNA. Yonath develops over two decades, together with collaborators, crystallization techniques specifically adapted to the ribosome's unusual flexibility and complexity. Venkatraman Ramakrishnan, a scientist of Indian origin working at the MRC Laboratory of Molecular Biology in Cambridge, and Thomas Steitz, at Yale University, independently and almost simultaneously complete in the year 2000 the first atomic-resolution structures of the two subunits of the bacterial ribosome, revealing in unprecedented detail how the molecule reads the genetic code and forms the chemical bonds between amino acids to build a protein. The structures also reveal, in great detail, the exact mechanism by which numerous clinically used antibiotics — including the streptomycin discovered by Waksman half a century earlier — bind to the bacterial ribosome to block its function without affecting the human ribosome, knowledge that directly guides the rational design of new antibiotics in the face of growing bacterial resistance.