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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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X-ray Crystallography02:18

X-ray Crystallography

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The size of the unit cell and the arrangement of atoms in a crystal may be determined from measurements of the diffraction of X-rays by the crystal, termed X-ray crystallography.
Diffraction
Diffraction is the change in the direction of travel experienced by an electromagnetic wave when it encounters a physical barrier whose dimensions are comparable to those of the wavelength of the light. X-rays are electromagnetic radiation with wavelengths about as long as the distance between neighboring...
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Interaction of EM Radiation with Matter: Spectroscopy01:12

Interaction of EM Radiation with Matter: Spectroscopy

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Electromagnetic (EM) radiation can be considered an oscillating electric and magnetic field propagating through a medium that can interact with matter in its path. The electric field in the radiation can interact with electrical charges in the atoms or molecules in the matter. On the other hand, the magnetic field can interact with the magnetic field in the atomic nucleus. The study of the interaction between electromagnetic radiation and matter is termed spectroscopy. Spectroscopy is the study...
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Dual Nature of Electromagnetic (EM) Radiation01:10

Dual Nature of Electromagnetic (EM) Radiation

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Electromagnetic (EM) radiation consists of electric and magnetic field components oscillating in planes perpendicular to each other and mutually perpendicular to radiation propagation through space. EM radiation can be classified as a wave, characterized by the properties of waves such as wavelength (denoted as λ) and frequency (represented by ν).
Wavelength is the distance between two consecutive peaks (the highest point) or troughs (the lowest point) in the wave. Frequency is the number of...
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Electron Carriers01:24

Electron Carriers

91.5K
Electron carriers can be thought of as electron shuttles. These compounds can easily accept electrons (i.e., be reduced) or lose them (i.e., be oxidized). They play an essential role in energy production because cellular respiration is contingent on the flow of electrons.
Over the many stages of cellular respiration, glucose breaks down into carbon dioxide and water. Electron carriers pick up electrons lost by glucose in these reactions, temporarily storing and releasing them into the electron...
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Electron Affinity03:07

Electron Affinity

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The electron affinity (EA) is the energy change for adding an electron to a gaseous atom to form an anion (negative ion).
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Related Experiment Video

Updated: Jan 27, 2026

Preparation of High-Temperature Sample Grids for Cryo-EM
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A new cryo-EM system for electron 3D crystallography by eEFD.

Koji Yonekura1, Tetsuya Ishikawa2, Saori Maki-Yonekura3

  • 1Biostructural Mechanism Laboratory, RIKEN, SPring-8 Center, 1-1-1 Kouto, Sayo, Hyogo 679-5148, Japan; Advanced Electron Microscope Development Unit, RIKEN-JEOL Collaboration Center, RIKEN Baton Zone Program, 1-1-1 Kouto, Sayo, Hyogo 679-5148, Japan.

Journal of Structural Biology
|April 1, 2019
PubMed
Summary

A new cryo-electron microscopy system enhances protein 3D crystallography using parallel illumination and energy filtration. This electron energy-filtered diffraction (eEFD) approach significantly improves data quality for protein complex structure determination.

Keywords:
CRYO ARMElectron 3D crystallographyEnergy filterParallEMeEFD

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A Robust Single-Particle Cryo-Electron Microscopy cryo-EM Processing Workflow with cryoSPARC, RELION, and Scipion
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A Robust Single-Particle Cryo-Electron Microscopy cryo-EM Processing Workflow with cryoSPARC, RELION, and Scipion

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Routine Collection of High-Resolution cryo-EM Datasets Using 200 KV Transmission Electron Microscope
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Routine Collection of High-Resolution cryo-EM Datasets Using 200 KV Transmission Electron Microscope

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Routine Collection of High-Resolution cryo-EM Datasets Using 200 KV Transmission Electron Microscope
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Routine Collection of High-Resolution cryo-EM Datasets Using 200 KV Transmission Electron Microscope

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Area of Science:

  • Structural Biology
  • Biophysics
  • Materials Science

Background:

  • Cryo-electron microscopy (cryo-EM) is crucial for determining protein structures.
  • Traditional cryo-EM faces limitations in data quality and resolution for certain samples.
  • Advancements in instrumentation are needed to overcome these challenges.

Purpose of the Study:

  • To develop and evaluate a novel cryo-EM system for enhanced protein electron 3D crystallography.
  • To assess the performance of electron energy-filtered diffraction (eEFD) for structural analysis.
  • To demonstrate the system's capability with protein complexes.

Main Methods:

  • A new cryo-EM system with parallel 300 kV electron beam illumination.
  • In-column energy filter for removing energy-loss electrons.
  • Rotational data collection on a fast camera.
  • Motorized cryo-sample loading and automated cooling.
  • Graphical User Interface (GUI) programs for operation and analysis.

Main Results:

  • Demonstrated improved data quality using eEFD compared to 200 kV data without filtration.
  • Successfully collected data for catalase and ExbBD membrane protein complex crystals.
  • Precise microscope control and automated processing of lens fluctuations were achieved.
  • Higher-energy electrons and energy filtration proved beneficial for electron 3D crystallography.

Conclusions:

  • The new cryo-EM system and eEFD approach significantly enhance data quality in protein electron 3D crystallography.
  • The system's automated features and advanced filtration enable more efficient and accurate structure determination.
  • This technology offers a promising path for resolving complex protein structures at higher resolution.