Cryo-EM

Cryo-electron microscopy (Cryo-EM) is a form of electron microscopy where the sample is studied at cryogenic temperatures. Cryo-EM is gaining popularity in structural biology. The development of this technique has been recognized with the Nobel Prize in Chemistry in 2017.

Overview[edit | edit source]

Cryo-EM is a type of electron microscopy in which the sample is cooled to cryogenic temperatures and is then examined in the electron microscope. This technique allows for the study of samples that would otherwise be damaged by the electron beam, such as biological specimens.

History[edit | edit source]

The development of Cryo-EM has been a gradual process that started in the 1980s. The technique was recognized with the Nobel Prize in Chemistry in 2017, awarded to Jacques Dubochet, Joachim Frank, and Richard Henderson for their work in developing cryo-electron microscopy for the high-resolution structure determination of biomolecules in solution.

Technique[edit | edit source]

In Cryo-EM, the sample is prepared by rapid freezing, a process known as vitrification. This preserves the sample in a near-native state without the need for chemical fixation or staining. The sample is then examined in the electron microscope at cryogenic temperatures.

Applications[edit | edit source]

Cryo-EM is particularly useful in structural biology, where it is used to determine the structure of a wide range of biological molecules and complexes. These include proteins, nucleic acids, and large molecular machines such as ribosomes and viruses.

References[edit | edit source]

Cryo-EM Resources
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