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Related Concept Videos

Cryo-electron Microscopy01:28

Cryo-electron Microscopy

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Conventional electron microscopy (EM) involves dehydration, fixation, and staining of biological samples, which distorts the native state of biological molecules and results in several artifacts. Also, the high-energy electron beam damages the sample and makes it difficult to obtain high-resolution images. These issues can be addressed using cryo-EM, which uses frozen samples and gentler electron beams. The technique was developed by Jacques Dubochet, Joachim Frank, and Richard Henderson, for...
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Transmission electron microscopy (TEM) can be used to determine the 3D structure of biological samples with the help of techniques such as electron microscope tomography and single-particle reconstruction. While single-particle reconstruction can examine macromolecules and macromolecular complexes in vitro conditions only, tomography permits the study of cell components or small cells in vivo.
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The cytoskeletal architecture can be studied using different microscopic and biochemical techniques. Electron microscopy was instrumental in discovering the cytoskeletal architecture around the 1960s, which allowed obtaining structural information at a high-resolution level. However, the sample preparation procedure often limits this ability in biological samples. Several protocols have been developed over the years to optimize sample preparation. In one of the protocols known as rotary...
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In 1931, physicist Ernst Ruska—building on the idea that magnetic fields can direct an electron beam just as lenses can direct a beam of light in an optical microscope—developed the first prototype of the electron microscope. This development led to the development of the field of electron microscopy. In the transmission electron microscope (TEM), electrons are produced by a hot tungsten element and accelerated by a potential difference in an electron gun, which gives them up to 400...
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The wavelengths of visible light ultimately limit the maximum theoretical resolution of images created by light microscopes. Most light microscopes can only magnify 1000X, and a few can magnify up to 1500X. Electrons, like electromagnetic radiation, can behave like waves, but with wavelengths of 0.005 nm, they produce significantly greater resolution up to 0.05 nm as compared to 500 nm for visible light. An electron microscope (EM) can create a sharp image that is magnified up to 2,000,000X.
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Enzymology and Dynamics by Cryogenic Electron Microscopy.

Ming-Daw Tsai1,2, Wen-Jin Wu1, Meng-Chiao Ho1,2

  • 1Institute of Biological Chemistry, Academia Sinica, Taipei, Taiwan;

Annual Review of Biophysics
|December 21, 2021
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Cryo-electron microscopy (cryo-EM) is transforming structural biology by revealing complex structures and dynamic processes. This technique offers new insights into enzymatic mechanisms and protein dynamics, advancing our understanding of biological functions.

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cryo-EMdynamicsenzymologystructural landscape

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Area of Science:

  • Structural biology
  • Biophysics
  • Biochemistry

Background:

  • Cryo-electron microscopy (cryo-EM) has significantly advanced structural biology, enabling the determination of complex molecular structures.
  • Its application is expanding into dynamic biological processes and enzymatic mechanisms.

Purpose of the Study:

  • To review the contribution and future potential of cryo-EM in studying enzymatic mechanisms and dynamic processes.
  • To highlight cryo-EM's capability in capturing multiple conformational and reaction states.
  • To compare cryo-EM with X-ray crystallography and NMR for these applications.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) for high-resolution structure determination.
  • Analysis of protein complexes under varying conditions (ligands, temperature, buffer).
  • Capturing transient states and reaction intermediates.

Main Results:

  • Cryo-EM can elucidate protein structures in multiple functional states and conditions.
  • It facilitates the study of dynamic conformational changes and enzymatic reaction pathways.
  • The technique provides a detailed structural landscape of proteins and complexes.

Conclusions:

  • Cryo-EM is a powerful tool for understanding enzymatic mechanisms and dynamic biological processes.
  • Its ability to capture multiple states expands structural biology's scope.
  • Cryo-EM offers unique advantages and complements traditional structural biology methods.