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To understand the biological processes underlying health and disease, it is essential to visualize the cells and molecules that are involved. Structural Biology aims to solve high-resolution structures of cells, organelles and enzymes in order to understand their function. Observing drug binding requires resolutions of 0.2-0.3 nanometers. Traditional light microscopes however, due to the wavelength of visible light, are physically limited to a resolution of 200 nanometers. Electrons and X-rays have a shorter wavelength, opening a door to the required resolution. But there are more challenges to be overcome: biomolecules are constantly in motion and highly sensitive to radiation. Freezing those molecules stops the motion and protects them from the radiation long enough to obtain high-resolution images in their native state.

For a long time, electron microscopy was hindered by the lack of cameras that are able to locate electrons precisely. The development of direct electron detectors in the 2000s lead to the so-called "resolution revolution". This novel type of camera finally allowed the precise detection of individual electrons and made cryo-Electron Microscopy a powerful tool in the field of structural biology. In the past 10 years, the number of protein structures that were solved by cryo-EM has continuously increased and it is on track to overtake X-ray crystallography as the #1 method in structural biology.

Furthermore, cryo-Electron Tomography is emerging as a unique tool for visualizing whole cells at high resolution and observing biomolecules in their native environment.