Abstract
Imaging a single biomolecule at atomic resolution without averaging over different conformations is the ultimate goal in structural biology. We report recordings of a protein at nanometer resolution obtained from one individual ferritin by means of low-energy electron holography. One single protein could be imaged for an extended period of time without any sign of radiation damage. Since the fragile protein shell encloses a robust iron cluster, the holographic reconstructions could also be cross-validated against transmission electron microscopy images of the very same molecule by imaging its iron core.