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Preparation of Samples for Electron Microscopy01:20

Preparation of Samples for Electron Microscopy

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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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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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Overview of Electron Microscopy01:25

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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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Scanning Electron Microscopy01:07

Scanning Electron Microscopy

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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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Immunogold Electron Microscopy01:20

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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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Cryo-electron Microscopy01:28

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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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Miniaturized Sample Preparation for Transmission Electron Microscopy
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Miniaturized Sample Preparation for Transmission Electron Microscopy.

Claudio Schmidli1, Luca Rima2, Stefan A Arnold1

  • 1Center for Cellular Imaging and NanoAnalytics (C-CINA), Biozentrum, University of Basel; Swiss Nanoscience Institute, University of Basel.

Journal of Visualized Experiments : Jove
|August 14, 2018
PubMed
Summary
This summary is machine-generated.

A new paper-blotting-free method uses microfluidics and nanoliter sample volumes for cryo-electron microscopy (cryo-EM) grid preparation. This technique optimizes sample handling, reduces consumption, and enables advanced applications like visual proteomics.

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Area of Science:

  • Structural Biology
  • Biophysics
  • Microscopy

Background:

  • Cryo-electron microscopy (cryo-EM) is crucial for high-resolution protein complex structural analysis.
  • Traditional EM sample preparation is a bottleneck, requiring large sample volumes and potentially harming proteins.
  • Miniaturized techniques are needed due to the large number of particles required for single-particle EM analysis.

Purpose of the Study:

  • To present a miniaturized, paper-blotting-free method for EM grid preparation using nanoliter sample volumes.
  • To overcome limitations of conventional EM sample preparation, reducing sample consumption and potential damage.
  • To enable novel experimental strategies in structural biology and proteomics.

Main Methods:

  • A dispensing system with sub-nanoliter precision for sample handling and EM grid priming.
  • A temperature-controlled platform to regulate humidity for sample film stabilization.
  • A pick-and-plunge mechanism for rapid sample vitrification in liquid ethane for cryo-EM.
  • Alternative methods for preparing nanoliter sample volumes for negative stain EM.

Main Results:

  • Successful preparation of EM grids using only nanoliter volumes of sample.
  • Demonstration of a paper-blotting-free method that avoids harmful procedures.
  • Controlled water evaporation for sample film thinning and stabilization.
  • Vitrification of samples for cryo-EM and preparation for negative stain EM.

Conclusions:

  • The developed method significantly reduces sample consumption for EM analysis.
  • This approach avoids detrimental effects on protein structure associated with traditional blotting techniques.
  • The technique facilitates advanced applications such as visual proteomics and quantitative analysis of complex samples.