Cryo-electron microscopy

Cryo-electron microscopy images biological specimens preserved at cryogenic temperatures using an electron microscope. It can reconstruct molecular structures from many particle images without crystallizing the specimen.

Vitrification: A process that solidifies water into a glass-like state without forming ice crystals. Rapid vitrification preserves hydrated specimens while limiting ice-crystal damage.
Electron: A negatively charged subatomic particle that carries current and interacts with matter. Electron beams provide image-forming signals but can also damage biological specimens.
Ernst Ruska: A German physicist who developed the electron microscope and shared the 1986 Nobel Prize in Physics. His electron-microscope work supplied the instrument lineage behind cryo-EM.
In situ cryo-electron tomography: A method that combines cryogenic electron tomography with focused-ion-beam specimen preparation to image cellular structures in place. It applies cryogenic imaging to molecular organization inside cells rather than purified particles.
X-ray crystallography: A method for determining atomic structures by analyzing X-ray diffraction from crystals. Unlike crystallography, many cryo-EM workflows do not require a crystal.
Transmission electron microscopy: Microscopy that forms images from electrons transmitted through a thin specimen. Cryogenic preparation adapts this imaging method to preserve biological structure.
Electron scattering: The deflection or energy change of electrons as they interact with matter. Scattering by specimen atoms generates the contrast used to infer structure.
Jacques Dubochet: A Swiss biophysicist who developed methods for vitrifying water in electron microscopy. His vitrification methods made hydrated biological specimens suitable for cryogenic imaging.
Cryo-electron tomography: A method that reconstructs three-dimensional views of frozen specimens from images collected at multiple tilt angles. It is suited to heterogeneous structures and molecular complexes in their cellular context.
Nuclear magnetic resonance spectroscopy: A method that uses nuclear magnetic resonance signals to study molecular structure and dynamics. NMR can probe molecular motion in solution, while cryo-EM often captures frozen structural populations.

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