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Related Concept Videos

Cryo-electron Microscopy01:28

Cryo-electron Microscopy

4.5K
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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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
Electron tomography can be performed either in TEM or STEM (scanning transmission...
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Related Experiment Video

Updated: Mar 7, 2026

Single Particle Cryo-Electron Microscopy: From Sample to Structure
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Single Particle Cryo-Electron Microscopy: From Sample to Structure

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Atomic-resolution structures from fragmented protein crystals with the cryoEM method MicroED.

M Jason de la Cruz1, Johan Hattne1, Dan Shi1

  • 1Howard Hughes Medical Institute, Janelia Research Campus, Ashburn, Virginia, USA.

Nature Methods
|February 14, 2017
PubMed
Summary
This summary is machine-generated.

Fragmenting large, imperfect protein crystals into microcrystals or nanocrystals offers a new method for high-resolution structure determination. This approach simplifies obtaining data using cryo-electron microscopy (cryoEM) and serial femtosecond crystallography.

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

  • Structural biology
  • Biophysics
  • Crystallography

Background:

  • Macromolecular crystallography traditionally requires large, well-ordered crystals, which are difficult to obtain.
  • Crystal imperfections can hinder high-resolution structure determination, even for sizable crystals.

Purpose of the Study:

  • To present a novel method for high-resolution structure determination of macromolecules.
  • To demonstrate the utility of crystal fragmentation for structure determination.

Main Methods:

  • Fragmentation of large, imperfect macromolecular crystals into microcrystals or nanocrystals.
  • Structure determination using cryo-electron microscopy (cryoEM) with Microcrystal Electron Diffraction (MicroED).
  • Potential application in serial femtosecond crystallography.

Main Results:

  • Crystal fragmentation provides a viable route to obtain high-resolution structural data.
  • MicroED enables high-resolution structure determination from fragmented crystals.

Conclusions:

  • Fragmenting imperfect crystals is a practical strategy for advancing macromolecular structure determination.
  • This technique expands the applicability of cryoEM and potentially serial femtosecond crystallography for challenging samples.