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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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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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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

Transmission Electron Microscopy

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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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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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Accelerated...
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Electron Microscope Tomography and Single-particle Reconstruction01:07

Electron Microscope Tomography and Single-particle Reconstruction

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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.
Electron Tomography
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Related Experiment Video

Updated: May 7, 2025

Cell Culture on Silicon Nitride Membranes and Cryopreparation for Synchrotron X-ray Fluorescence Nano-analysis
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Cryoelectron microscopy with elemental sensitivity.

Hannah Ochner1, Tanmay A M Bharat1

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Researchers developed a new technique combining electron energy-loss spectroscopy and cryo-electron microscopy for elemental mapping of macromolecules. This method provides spatially resolved insights into molecular composition.

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Area of Science:

  • Structural biology
  • Biophysics
  • Analytical chemistry

Background:

  • Understanding the elemental composition of macromolecules is crucial for elucidating their structure and function.
  • Existing techniques often lack the spatial resolution or elemental specificity required for detailed analysis.

Purpose of the Study:

  • To develop and demonstrate a novel correlative imaging approach for high-resolution elemental mapping of biological macromolecules.
  • To enable the investigation of elemental distribution within complex molecular assemblies.

Main Methods:

  • Correlative imaging combining electron energy-loss spectroscopy (EELS) with single-particle cryo-electron microscopy (cryo-EM).
  • Spatially resolved EELS acquisition on cryo-EM grids to determine elemental composition.
  • Integration of spectroscopic data with structural information from cryo-EM.

Main Results:

  • Successful spatially resolved elemental mapping of macromolecules was achieved.
  • Demonstrated the ability to identify and localize specific elements within macromolecular structures.
  • The combined approach provides unprecedented detail on elemental distribution.

Conclusions:

  • The integrated EELS and cryo-EM technique offers a powerful new tool for structural and compositional analysis of macromolecules.
  • This method opens new avenues for studying the roles of specific elements in biological processes at the nanoscale.
  • Future applications include analyzing metalloproteins, nucleic acids, and other elemental-containing biomolecules.