David A. Agard

Professor of Biochemistry and Biophysics. With Sedat, developed 3D deconvolution fluorescence light microscopy used throughout the world for biological imaging, developed structured illumination microscopy and other super-resolution methods that extend resolution by at least two-fold. With Cheng, empowered the "resolution revolution" in cryo-electron microscopy by co-dveloping the first single electron counting camera for EM and developed powerful software methods to remove beam-induced image blurring in cryoEM.  Redefined mechanisms of microtubule nucleation and growth, defined the molecular mechanism the roles of the molecular chaperone Hsp90 in the the folding and activation of 10% of the proteome.