The abundance of high-resolution structural information on biological molecules in their native states that emerged in the past decade has been the result of three revolutions: in the first (“single-particle techniques”), the very concept of structure was generalized and freed from the necessity of crystallization; in the second (“cryo-EM”), a mode of sample preparation was invented that kept the molecule in its native, hydrated state; and in the third (“direct electron detection”), the sensitivity and resolution of image recording in the electron microscope was boosted by the invention of new cameras, bringing us the current level of spatial resolution in the range of 2-4 Angstrom. More recent developments are geared toward the recovery of information on the dynamics of molecules.
Joachim Frank is a professor at  the Department of Biochemistry and Molecular Biophysics, and Professor at the Department of Biological Sciences, Columbia University.

Joachim Frank was born in 1940 and raised in post-war Germany. Discovering twisted copper wires and Bakelite panels in the rubble of ruins as a young boy gave him the first inspirations toward his later career choice, followed by “experiments” under the verandah of his parents’ house.  As he later during his work toward a Ph.D. learned about electron microscopy and started digital image processing, an idée fixe took hold of his mind: the idee that structure determination of molecules should not require their arrangement in perfect order, as in crystals.  To see this idea of “single particle reconstruction” blossom and develop into a new branch of structural biology has been a most gratifying experience in the past 50 years, and particularly the past decade.


Portrætfoto: Jorg Meyer/Columbia University Medical Center