Here surprising results are shown demonstrating a workflow possibly able to exploit the discreet nature of interactions between high-energy electron beams and matter. Isolated protein constructs have been imaged after an original temperature-curing in vacuum, introduced recently for flash-frozen rigid biopolymers, and here applied to flash-frozen oligomers of viral origin. These results, if confirmed, may extend to plastics and bio-oligomers the access to atomic coordinates in one experimental session, when imaged by electron microscopy. Which is the case when imaging semiconductors or other solid materials, provided that the samples are not damaged by the interaction with accelerated electron beams in vacuum. Therefore, potentially, this workflow introduces the possibility of achieving atomic resolution in only one experiment with data only about one individual protein, maybe out of thermodynamic equilibrium. Such data are vital to understand protein-protein interactions. Finally, this workflow offers the possibility, new to cryo-electron microscopy samples, to store a sample indefinitely under liquid nitrogen for imaging the same molecules in more than one experimental session.