scholarly journals Unravelling biological macromolecules with cryo-electron microscopy

Nature ◽  
2016 ◽  
Vol 537 (7620) ◽  
pp. 339-346 ◽  
Author(s):  
Rafael Fernandez-Leiro ◽  
Sjors H. W. Scheres
Keyword(s):  
Electron Microscopy ◽  
Biological Macromolecules ◽  
Cryo Electron Microscopy

Dynamic behavior of biomaterials uncovered by cryo-electron microscopy.

2020 ◽  
Vol 23 ◽  
Author(s):  
Yimin Zhao ◽  
Yizhen Zhao ◽  
Bingquan Peng ◽  
Lei Zhang
Keyword(s):  
Electron Microscopy ◽  
Protein Interactions ◽  
Rapid Development ◽  
Conformational Space ◽  
Biological Macromolecules ◽  
Protein Protein Interactions ◽  
Static Structure ◽  
Cryo Electron Microscopy ◽  
Biological Complexes ◽  
Functional Mechanisms

: Structural biology develops rapidly as time goes on. Based only on static structure analysis of biomaterials is not enough to satisfy the studies of their functional mechanisms, with a huge obstacle for the dynamic process of biological complexes. The rapid development of cryo-electron microscopy(cryo-EM) technology makes that it is possible to observe the near-atomic resolution structures and dynamic nature of biological macromolecules, in the fields of dynamic characteristics of proteins, protein-protein interactions, molecular recognition, and structure-based design. In this review, we systematically elaborate the contribution of cryo-EM technology in the field of biomaterials such as ribosome motion, membrane protein structure and conformational space, dynamic transmission within the plasma membrane and clinical applications. We also put forwards a new standpoint in the development of cryo-EM technology.

scholarly journals A WAVELET BASED ALTERNATIVE ITERATION METHOD FOR THE ORIENTATION REFINEMENT OF CRYO-ELECTRON MICROSCOPY 3D RECONSTRUCTION

2015 ◽  
Vol 20 (3) ◽  
pp. 396-408 ◽  
Author(s):  
Zhucui Jing ◽  
Ming Li
Keyword(s):  
Electron Microscopy ◽  
Iteration Method ◽  
Three Dimensional ◽  
Particle Method ◽  
Biological Macromolecules ◽  
Orthonormal Bases ◽  
Cryo Electron Microscopy ◽  
Marquardt Algorithm ◽  
Density Map ◽  
Particle Images

Cryo-electron microscopy (cryo-EM) single particle method (SPM) reconstructs the three-dimensional (3D) density map of biological macromolecules using 2D particle images with estimated orientations. The estimated orientations have errors which result in the decrease in resolution of the reconstructed map. We propose a wavelet orthonormal bases based iteration method by refining alternatively the orientations and the map using Levenberg–Marquardt algorithm and soft-thresholding, respectively. The convergence analysis of the proposed algorithm is provided and numerical experiments for simulated particle images show its good performance.

scholarly journals Introduction to high-resolution cryo-electron microscopy

2016 ◽  
Vol 62 (3) ◽  
pp. 383-394
Author(s):  
Mariusz Czarnocki-Cieciura ◽  
Marcin Nowotny
Keyword(s):  
Electron Microscopy ◽  
Nmr Spectroscopy ◽  
Structural Biology ◽  
Atomic Resolution ◽  
Biological Macromolecules ◽  
X Ray ◽  
X Ray Crystallography ◽  
Cryo Electron Microscopy ◽  
Transmission Electron ◽  
Electron Microscopes

For many years two techniques have dominated structural biology – X-ray crystallography and NMR spectroscopy. Traditional cryo-electron microscopy of biological macromolecules produced macromolecular reconstructions at resolution limited to 6–10 Å. Recent development of transmission electron microscopes, in particular the development of direct electron detectors, and continuous improvements in the available software, have led to the “resolution revolution” in cryo-EM. It is now possible to routinely obtain near-atomic-resolution 3D maps of intact biological macromolecules as small as ~100 kDa. Thus, cryo-EM is now becoming the method of choice for structural analysis of many complex assemblies that are unsuitable for structure determination by other methods.

Organized packing of RNA inside viruses as revealed by cryo-electron microscopy and x-ray diffraction analysis

1992 ◽  
Vol 50 (1) ◽  
pp. 454-455
Author(s):  
T. S. Baker ◽  
R. H. Cheng ◽  
J. E. Johnson ◽  
N. H. Olson ◽  
G. J. Wang ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Diffraction Analysis ◽  
Three Dimensional ◽  
Biological Macromolecules ◽  
Three Dimensional Reconstruction ◽  
X Ray Diffraction ◽  
X Ray ◽  
Cryo Electron Microscopy ◽  
Dimensional Reconstruction ◽  
Microscopy Techniques

The development of modern electron microscopy techniques to visualize the hydrated structures of biological macromolecules has stimulated many new studies, especially with viruses and virus-macromolecule complexes that are too large to study with current x-ray crystallographic methods, Cryo-electron microscopy (cryoEM) in conjunction with three-dimensional reconstruction procedures is capable of revealing both external and internal features of these structures.

scholarly journals Visualization of biological macromolecules at near-atomic resolution: cryo-electron microscopy comes of age

2019 ◽  
Vol 75 (1) ◽  
pp. 3-11 ◽  
Author(s):  
Alok K. Mitra
Keyword(s):  
Electron Microscopy ◽  
Structural Biology ◽  
Atomic Resolution ◽  
Particle Analysis ◽  
Biological Macromolecules ◽  
Single Particles ◽  
Cryo Electron Microscopy ◽  
Electron Microscopes ◽  
Resolution Single ◽  
Resolution Structure

Structural biology is going through a revolution as a result of transformational advances in the field of cryo-electron microscopy (cryo-EM) driven by the development of direct electron detectors and ultrastable electron microscopes. High-resolution cryo-EM images of isolated biomolecules (single particles) suspended in a thin layer of vitrified buffer are subjected to powerful image-processing algorithms, enabling near-atomic resolution structures to be determined in unprecedented numbers. Prior to these advances, electron crystallography of two-dimensional crystals and helical assemblies of proteins had established the feasibility of atomic resolution structure determination using cryo-EM. Atomic resolution single-particle analysis, without the need for crystals, now promises to resolve problems in structural biology that were intractable just a few years ago.

Preparing Better Samples for Cryo–Electron Microscopy: Biochemical Challenges Do not End with Isolation and Purification

2021 ◽  
Vol 90 (1) ◽  
Author(s):  
Robert M. Glaeser
Keyword(s):  
Electron Microscopy ◽  
High Resolution Electron Microscopy ◽  
Effective Control ◽  
Annual Review ◽  
Publication Date ◽  
Biological Macromolecules ◽  
Isolation And Purification ◽  
Cryo Electron Microscopy ◽  
Extreme Risk ◽  
Resolution Electron

The preparation of extremely thin samples, which are required for high-resolution electron microscopy, poses extreme risk of damaging biological macromolecules due to interactions with the air-water interface. Although the rapid increase in the number of published structures initially gave little indication that this was a problem, the search for methods that substantially mitigate this hazard is now intensifying. The two main approaches under investigation are ( a) immobilizating particles onto structure-friendly support films and ( b) reducing the length of time during which such interactions may occur. While there is little possibility of outrunning diffusion to the interface, intentional passivation of the interface may slow the process of adsorption and denaturation. In addition, growing attention is being given to gaining more effective control of the thickness of the sample prior to vitrification. Expected final online publication date for the Annual Review of Biochemistry, Volume 90 is June 2021. Please see http://www.annualreviews.org/page/journal/pubdates for revised estimates.

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