Cryo-electron microscopy
Cryo-electron microscopy (pronunciation: kryo-electron microscopy, from the Greek kryos meaning cold, electron meaning amber, and microscopy meaning to view in detail) is a form of Electron microscopy that involves freezing the sample to be observed, which allows for the preservation of its natural structure.
Overview
Cryo-electron microscopy is a technique used to image frozen-hydrated specimens at cryogenic temperatures. The technique is particularly useful for the high-resolution structural determination of biomolecules, especially proteins.
History
The development of cryo-electron microscopy can be traced back to the 1980s, with significant advancements in the field occurring in the 21st century. The 2017 Nobel Prize in Chemistry was awarded to Jacques Dubochet, Joachim Frank, and Richard Henderson for their work in developing cryo-electron microscopy.
Technique
The technique involves rapidly freezing a thin layer of the sample, which is then viewed under an electron microscope. The rapid freezing prevents the formation of ice crystals, which can damage the sample. The sample is maintained at cryogenic temperatures throughout the imaging process.
Applications
Cryo-electron microscopy has a wide range of applications in the field of Structural biology. It is used to study the structure of various biological specimens, including viruses, bacteria, and cells. It is also used in the study of protein structure and protein-protein interactions.
Advantages and Limitations
The main advantage of cryo-electron microscopy is that it allows for the observation of specimens in their natural state, without the need for dyes or fixatives. However, the technique requires specialized equipment and expertise, and the preparation of samples can be challenging.
See Also
External links
- Medical encyclopedia article on Cryo-electron microscopy
- Wikipedia's article - Cryo-electron microscopy
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