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Overview of Electron Microscopy01:25

Overview of Electron Microscopy

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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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A scanning electron microscope (SEM) is used to study the surface features of a sample by using an electron beam that scans the sample surface in a two-dimensional manner. Typically, areas between ~1 centimeter to 5 micrometers in width can be imaged. SEM can be used to image bacteria, viruses, tissues as well as larger samples like insects. Conventional SEM gives a magnification ranging from 20X to 30,000X and spatial resolution of 50 to 100 nanometers.
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Transmission Electron Microscopy01:15

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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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Immunoelectron microscopy utilizes immunogold labeling of endogenous proteins with specific antibodies to detect and localize these proteins in cells and tissues. The procedure provides insights into the distribution and quantification of protein under different stimulation conditions offering clues about their functions. Conjugating highly electron-dense gold particles with primary or secondary antibodies allow antigen detection on and within cells, with high resolution and specificity.
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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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To be visualized by an electron microscope, either transmission or scanning, biological samples need to be fixed (stabilized) so the electron beam does not destroy them and dried thoroughly (desiccated/dehydrated) so the vacuum does not affect them. Fixation needs to be done as quickly as possible because the sample properties will start changing as soon as it is removed from its natural environment. For example, in a tissue sample, the oxygen levels begin decreasing, causing an altered...
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Advances in domain and subunit localization technology for electron microscopy.

Zuben P Brown1, Junichi Takagi2

  • 1Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY, USA. zb2218@cumc.columbia.edu.

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Summary

Cryo-electron microscopy (cryo-EM) determines high-resolution biomolecule structures. When cryo-EM yields intermediate resolution, the PA tag/NZ-1 antibody system aids in understanding macro-level protein complex organization.

Keywords:
Domain mappingElectron microscopyNZ-1PA tag

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Area of Science:

  • Structural Biology
  • Biochemistry
  • Microscopy

Background:

  • Cryo-electron microscopy (cryo-EM) has revolutionized structural biology, enabling high-resolution determination of biomolecules.
  • Advances in equipment and techniques allow atomic-level structural assessment of complex biological machinery.
  • However, not all biological targets are amenable to high-resolution cryo-EM analysis, often resulting in intermediate resolution structures.

Purpose of the Study:

  • To review methods for characterizing protein/biomolecular complex organization at the macro-level when high-resolution structures are unavailable.
  • To highlight the utility of complementary techniques for understanding domain or subunit orientation.
  • To introduce a novel protein purification approach, the PA tag/NZ-1 antibody system, for electron microscopy.

Main Methods:

  • Review of various biophysical and biochemical techniques.
  • Discussion of electron microscopy (EM) applications.
  • Detailed examination of the PA tag/NZ-1 antibody system for protein purification in EM.

Main Results:

  • Identification of complementary methods for macro-level structural analysis.
  • Demonstration of the PA tag/NZ-1 antibody system's beneficial properties for EM experiments.
  • Improved characterization of protein complexes at intermediate resolutions.

Conclusions:

  • Complementary methods are essential for understanding biomolecular architecture when high-resolution data is limited.
  • The PA tag/NZ-1 antibody system offers a valuable tool for enhancing protein purification and structural determination in EM.
  • Further application of these techniques will advance the study of complex biological systems.