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Related Concept Videos

Preparation of Samples for Electron Microscopy01:20

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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 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.
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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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Related Experiment Video

Updated: Nov 29, 2025

Optimizing Sample Preparation for Cryogenic Electron Microscopy
06:32

Optimizing Sample Preparation for Cryogenic Electron Microscopy

Published on: April 11, 2025

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Native Mass Spectrometry-Based Screening for Optimal Sample Preparation in Single-Particle Cryo-EM.

Paul Dominic B Olinares1, Jin Young Kang2, Eliza Llewellyn2

  • 1Laboratory of Mass Spectrometry and Gaseous Ion Chemistry, The Rockefeller University, New York, NY 10065, USA.

Structure (London, England : 1993)
|November 20, 2020
PubMed
Summary
This summary is machine-generated.

Native mass spectrometry (nMS) rapidly assesses protein complex quality for structural biology. This method streamlines sample preparation, accelerating cryogenic electron microscopy (cryo-EM) studies of vital biological assemblies.

Keywords:
SARS-CoV-2 replication-transcription complexbacterial RNA polymerasebiochemical screeningcryo-EMcryo-EM sample quality checkintegrated structural biologynative mass spectrometryprotein complexestranscription

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Area of Science:

  • Structural Biology
  • Biochemistry
  • Biophysics

Background:

  • Single-particle cryogenic electron microscopy (cryo-EM) offers high-resolution structural insights into protein assemblies.
  • Cryo-EM is time-consuming and resource-intensive, necessitating efficient sample quality assessment.
  • Rapid evaluation of sample integrity and homogeneity is crucial for successful cryo-EM studies.

Purpose of the Study:

  • To develop a rapid platform for assessing protein complex quality before cryo-EM analysis.
  • To streamline biochemical screening and optimize sample preparation for structural determination.
  • To facilitate cryo-EM studies by providing early feedback on sample characteristics.

Main Methods:

  • Development of a native mass spectrometry (nMS) platform.
  • Utilizing nMS for accurate mass analysis of protein complexes.
  • Applying nMS for routine evaluation of sample composition, integrity, and homogeneity.

Main Results:

  • The nMS platform provides rapid feedback on sample quality.
  • Biochemical screening is highly streamlined using the nMS approach.
  • Demonstrated utility in facilitating cryo-EM studies of bacterial transcription complexes and SARS-CoV-2 replication-transcription assembly.

Conclusions:

  • Native mass spectrometry is a valuable tool for rapid sample quality assessment in structural biology.
  • The developed nMS platform accelerates and optimizes the workflow for cryo-EM studies.
  • This approach enhances the efficiency of determining structures of important biological complexes, including viral components.