Electron tomography studies proteins and cells with imaging technologies based on advanced transmission electron microscopy (TEM). Researchers confront a stubborn, multidimensional gap in which technological deficiencies along at least three different axes coincide:
- The simplest of the gaps is in imaging and analysis of the spatial resolution falling between the atomic resolution of NMR and XRD and the cellular resolution of light microscopy, a critical spatial regime that includes large molecules and multi-molecular complexes.
- The second gap occurs between the natural, living context of in vivo analysis and the artificial context of isolated, purified, crystallized molecular preparations.
- The final gap exists between modeling systems used to discover and develop new drugs, and the biological systems the models are intended to imitate.
Electron tomography bridges the gaps described above. Its resolution at the nanometer level falls between the sub-Ångström resolution of XRD and NMR and the sub-micrometer scale of light microscopy. It is sufficient to resolve the tertiary and quaternary structure of proteins, protein complexes and cellular structures.