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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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Protein and Protein Structure02:15

Protein and Protein Structure

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Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
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Electronic Structure of Atoms02:28

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An atom comprises protons and neutrons, which are contained inside the dense, central core called the nucleus, with electrons present around the nucleus. Taking into account the wave–particle duality of electrons and the uncertainty in position around the nucleus, quantum mechanics provides a more accurate model for the atomic structure. It describes atomic orbitals as the regions around the nucleus where electrons of discrete energy exist, characterized by four quantum...
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Structural Protein Function01:56

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Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
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Overview of Electron Microscopy01:25

Overview of Electron Microscopy

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The wavelengths of visible light ultimately limit the maximum theoretical resolution of images created by light microscopes. Most light microscopes can only magnify 1000X, and a few can magnify up to 1500X. Electrons, like electromagnetic radiation, can behave like waves, but with wavelengths of 0.005 nm, they produce significantly greater resolution up to 0.05 nm as compared to 500 nm for visible light. An electron microscope (EM) can create a sharp image that is magnified up to 2,000,000X.
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Scanning Electron Microscopy01:07

Scanning Electron Microscopy

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A scanning electron microscope (SEM) is used to study the surface features of a sample by using an electron beam that scans the sample surface in a two-dimensional manner. Typically, areas between ~1 centimeter to 5 micrometers in width can be imaged. SEM can be used to image bacteria, viruses, tissues as well as larger samples like insects. Conventional SEM gives a magnification ranging from 20X to 30,000X and spatial resolution of 50 to 100 nanometers.
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Author Spotlight: Enhancing CryoEM Sample Preparation Using Graphene Monolayer on Microscopy Grids
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Simultaneous Determination of Protein Structure and Dynamics Using Cryo-Electron Microscopy.

Massimiliano Bonomi1, Riccardo Pellarin2, Michele Vendruscolo1

  • 1Department of Chemistry, University of Cambridge, Cambridge, United Kingdom.

Biophysical Journal
|April 12, 2018
PubMed
Summary

This study introduces a new integrative modeling method to analyze cryo-electron microscopy data, revealing both structure and dynamics of complex biological molecules. This approach enhances understanding of macromolecular function, exemplified by insights into the STRA6 receptor.

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Single Particle Cryo-Electron Microscopy: From Sample to Structure
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Area of Science:

  • Structural Biology
  • Biophysics
  • Computational Biology

Background:

  • Cryo-electron microscopy (cryo-EM) is a powerful tool for determining macromolecular structures.
  • Understanding the dynamics and movements of these structures is crucial for elucidating biological functions.
  • Existing methods often struggle to capture the dynamic nature of macromolecular systems from cryo-EM data.

Purpose of the Study:

  • To develop an integrative modeling approach for simultaneously determining structure and dynamics from cryo-EM density maps.
  • To enable the modeling of structural ensembles and population inference from noisy, averaged cryo-EM data.
  • To provide mechanistic insights into the function of the STRA6 receptor and its interaction with retinol binding protein.

Main Methods:

  • Developed an integrative modeling approach to process cryo-EM density maps.
  • Quantified data noise and addressed the ensemble-averaged nature of cryo-EM data.
  • Integrated multiple information sources to model structural ensembles and their populations.

Main Results:

  • Successfully determined the structure and dynamics of the integral membrane receptor STRA6.
  • Provided insights into the interaction mechanisms between STRA6 and retinol binding protein.
  • Offered a deeper understanding of retinol translocation across the membrane mediated by STRA6.

Conclusions:

  • The developed integrative modeling approach effectively characterizes both structure and dynamics from cryo-EM data.
  • This method advances the study of dynamic macromolecular systems, crucial for understanding biological mechanisms.
  • The findings illuminate the functional mechanisms of the STRA6 receptor in retinol transport.