Jane S. Richardson and her husband David have worked together for over 50 years on research to understand the 3D structure of protein and RNA molecules, including their description, determinants, folding, evolution, and control. They were among the early groups doing protein crystallography, helped to start the field of protein de novo design, and developed the molecular graphics system of "kinemages". Around 2000 they developed a method that calculates hydrogen-atom contacts to visualize and quantify the details of packing interactions inside and between molecules. Its principal application is to improving the accuracy of experimental structures of protein and RNA molecules, as implemented on their MolProbity structure-validation web service and within the Phenix software system for crystallography & cryoEM, and used to help depositors re-version early-release SARS-COV-2 structures. They are now working on validation methods that can still find errors when previous validation criteria are being refined or restrained. Prof. Richardson pioneered ribbon drawings for representing protein structures, first described many of the common features of overall protein folds and their local motifs (such as Greek key beta barrels, righthanded crossovers, helix caps, cis Pro touch-turns, vicinal disulfides) and has worked to spread molecular 3D literacy to students and colleagues at Duke and around the world. From a Swarthmore B.A. in math, physics, astronomy and philosophy, she has become a biophysicist, a MacArthur Fellow, a member of the National Academies of Sciences & of Medicine, and a James B. Duke Professor of Biochemistry at Duke, and has three honorary degrees to fill in for her lack of a PhD. For more details, see Ann. Rev. Biophysics (2013) 4:1-28 or J. Biol. Chem. (2021) 296:100742.