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Related Concept Videos

Cryo-electron Microscopy01:28

Cryo-electron Microscopy

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

Electron Microscope Tomography and Single-particle Reconstruction

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
Electron tomography can be performed either in TEM or STEM (scanning transmission...

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Related Experiment Video

Updated: May 11, 2026

Do's and Don'ts of Cryo-electron Microscopy: A Primer on Sample Preparation and High Quality Data Collection for Macromolecular 3D Reconstruction
09:25

Do's and Don'ts of Cryo-electron Microscopy: A Primer on Sample Preparation and High Quality Data Collection for Macromolecular 3D Reconstruction

Published on: January 9, 2015

Imaging protein three-dimensional nanocrystals with cryo-EM.

Igor Nederlof1, Yao Wang Li, Marin van Heel

  • 1Leiden Institute of Chemistry, Leiden University, Einsteinweg 55, 2333 CC Leiden, The Netherlands.

Acta Crystallographica. Section D, Biological Crystallography
|May 2, 2013
PubMed
Summary

Cryo-electron microscopy (cryo-EM) successfully imaged 3D protein nanocrystals, achieving 2 Å resolution. This technique shows promise for determining the 3D structures of delicate protein crystals.

Keywords:
electron microscopyprotein nanocrystals

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Last Updated: May 11, 2026

Do's and Don'ts of Cryo-electron Microscopy: A Primer on Sample Preparation and High Quality Data Collection for Macromolecular 3D Reconstruction
09:25

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Correlative Microscopy for 3D Structural Analysis of Dynamic Interactions
13:43

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Published on: June 24, 2013

Area of Science:

  • Structural biology
  • Biophysics
  • Materials science

Background:

  • Three-dimensional protein nanocrystals are challenging to study due to their small size and sensitivity.
  • High-resolution imaging of biological materials requires advanced electron microscopy techniques.

Purpose of the Study:

  • To assess the feasibility of using cryo-electron microscopy (cryo-EM) for high-resolution imaging of 3D protein nanocrystals.
  • To evaluate the potential of direct electron detectors for capturing structural information from these delicate samples.

Main Methods:

  • Flash-cooled 3D lysozyme nanocrystals (approx. 100 nm thick) were imaged using 300 kV cryo-EM.
  • A Falcon direct electron detector was employed to record images near focus.
  • Fourier transforms and advanced data processing were used to analyze the images.

Main Results:

  • Reciprocal lattice information was obtained up to 3 Å resolution in some cases, and 4 Å resolution for about half the crystals.
  • Analysis revealed non-uniform crystal ordering and the presence of multiple mosaic blocks within crystals.
  • Data processing enabled the resolution of details finer than 2 Å.

Conclusions:

  • Cryo-EM imaging of 3D protein nanocrystals is a viable method for structural analysis.
  • Direct electron detectors facilitate high-resolution data acquisition from these samples.
  • Further development could enable full 3D structure determination of protein nanocrystals.