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Related Concept Videos

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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Sample Preparation for Analysis: Overview01:21

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Sample preparation is an essential step in the analytical process. It involves preparing a sample so that it can be analyzed accurately. The goal is to extract the analyte, the substance you want to measure, from the sample while removing any components that may interfere with the analysis. Sample preparation techniques vary depending on the physical state of the sample.
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Interaction of EM Radiation with Matter: Spectroscopy01:12

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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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Accurate analysis of complex samples often requires advanced preparation techniques to achieve reliable and reproducible results. Samples containing inorganic or organic materials can be challenging to dissolve or decompose effectively. Standard sample preparation methods include acid digestion, fusion, dry ashing, and wet digestion.
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Dual Nature of Electromagnetic (EM) Radiation01:10

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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).
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Cryo-electron Microscopy01:28

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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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Microfluidic protein isolation and sample preparation for high-resolution cryo-EM.

Claudio Schmidli1,2, Stefan Albiez1, Luca Rima1

  • 1Center for Cellular Imaging and Nanoanalytics, Biozentrum, 4058 Basel, Switzerland.

Proceedings of the National Academy of Sciences of the United States of America
|July 12, 2019
PubMed
Summary

Researchers developed a microfluidic method for rapid protein isolation and preparation for cryogenic electron microscopy (cryo-EM). This technique uses minimal cell lysate to determine high-resolution protein structures, enabling high-throughput studies.

Keywords:
cryo-EMendogenousmicrofluidicsprotein purificationsample preparation

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Area of Science:

  • Structural Biology
  • Biochemistry
  • Biophysics

Background:

  • High-resolution protein structures are crucial for understanding biological functions.
  • Traditional protein structure determination methods require large protein quantities and extensive purification.
  • Cryogenic electron microscopy (cryo-EM) requires fewer protein particles but obtaining sufficient quantities remains a challenge.

Purpose of the Study:

  • To develop a microfluidic method for rapid isolation and direct preparation of target proteins for cryo-EM.
  • To demonstrate the utility of this method for determining the structure of endogenous, untagged proteins from minimal sample volumes.

Main Methods:

  • A novel microfluidic system was employed for the rapid isolation of target proteins from cell lysate.
  • The isolated proteins were directly prepared for cryo-EM analysis without extensive purification.
  • The method was applied to determine the atomic structure of the human 20S proteasome.

Main Results:

  • The microfluidic method successfully isolated target proteins and prepared them for cryo-EM.
  • The atomic structure of the untagged, endogenous human 20S proteasome was determined using less than 1 μL of cell lysate.
  • This demonstrates the feasibility of structure determination from minimal biological samples.

Conclusions:

  • The developed microfluidic method enables rapid, high-throughput protein structure determination using minimal sample input.
  • This approach facilitates the study of sensitive and endogenous protein complexes that are difficult to isolate in large quantities.
  • The findings open new avenues for structural biology research, particularly for challenging protein targets.