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Exploring cryo-electron microscopy with molecular dynamics
Biochemical Society Transactions, 2022Single particle analysis cryo-electron microscopy (EM) and molecular dynamics (MD) have been complimentary methods since cryo-EM was first applied to the field of structural biology. The relationship started by biasing structural models to fit low-resolution cryo-EM maps of large macromolecular complexes not amenable to crystallization.
John W. Vant +5 more
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Brain and nerve = Shinkei kenkyu no shinpo, 2019
Cryo-electron microscopy (cryo-EM) includes three technical methods, (1) rapid freezing for vitreous ice-embedding, (2) observation of frozen hydrated specimens, and (3) image processing for three-dimensional structural analysis. The three-dimensional structural analysis can be performed in three different ways.
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Cryo-electron microscopy (cryo-EM) includes three technical methods, (1) rapid freezing for vitreous ice-embedding, (2) observation of frozen hydrated specimens, and (3) image processing for three-dimensional structural analysis. The three-dimensional structural analysis can be performed in three different ways.
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Conventional Electron Microscopy, Cryo-Electron Microscopy and Cryo-Electron Tomography of Viruses
2013Electron microscopy (EM) techniques have been crucial for understanding the structure of biological specimens such as cells, tissues and macromolecular assemblies. Viruses and related viral assemblies are ideal targets for structural studies that help to define essential biological functions.
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Single-particle cryo-electron microscopy
Nature Methods, 2015A brief overview of how to solve a macromolecular structure using single-particle cryo-electron microscopy (cryo-EM).
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Cryo Electron Microscopy of TRP Channels
2019Cryo electron microscopy (cryo-EM) is a powerful technique that can be used to elucidate the structural architecture of a protein molecule in a physiologically relevant environment. In this method, purified protein is frozen in its aqueous buffer in a thin layer of vitreous ice in which the biological macromolecules are embedded in various orientations.
Amrita, Samanta +2 more
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Cryo-electron Microscopy of Vitreous Sections
2013More than 30 years ago two groups independently reported the vitrification of pure water, which was until then regarded as impossible without a cryoprotectant [1, 2]. This opened the opportunity to cryo-electron microscopy (cryo-EM) to observe biological samples at nanometer scale, close to their native state. However, poor electron penetration through
Petr, Chlanda, Martin, Sachse
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Cryo-electron microscopy of GDP-tubulin rings
Cell Biochemistry and Biophysics, 1999Rings of guanosine diphosphate (GDP)-tubulin formed in the presence of divalent cations have been studied using conventional negative stain and cryo-electron microscopy. The structure of such rings resembles that of depolymerizing microtubule ends and corresponds to an "unconstrained" conformation of tubulin in its GDP state. The use of cryo-techniques
Nicholson, William V. +3 more
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Cryo-Electron Microscopy of DNA
1994Seeing is believing! Less than 10 years after the discovery of the double helical structure of the DNA, the development by Kleinschmidt and Zahn (Kleinschmidt and Zahn 1959) of a method for direct visualization of nucleic acids has been and remains one of the major achievement of electron microscopy.
J. Dubochet +3 more
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Observation of Bacteriophage Ultrastructure by Cryo-electron Microscopy
2017Transmission Electron Microscopy (TEM) is an ideal method to observe and determine the structure of bacteriophages. From early studies by negative staining to the present atomic structure models derived from cryo-TEM, bacteriophage detection, classification, and structure determination has been mostly done by electron microscopy.
Ana, Cuervo, José L, Carrascosa
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Grid Preparation for Cryo-Electron Microscopy
2012Once 2D crystals suitable for electron crystallography have been obtained, grid preparation for cryo-EM is a critical step in obtaining high-resolution structural information. Specimens have to be prepared in a manner that prevents dehydration and disruption of the crystals in the vacuum of the electron microscope.
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