The Resolution Revolution

  title={The Resolution Revolution},
  author={Werner K{\"u}hlbrandt},
  pages={1443 - 1444}
Advances in detector technology and image processing are yielding high-resolution electron cryo-microscopy structures of biomolecules. [Also see Report by Amunts et al.] Precise knowledge of the structure of macromolecules in the cell is essential for understanding how they function. Structures of large macromolecules can now be obtained at near-atomic resolution by averaging thousands of electron microscope images recorded before radiation damage accumulates. This is what Amunts et al. have… 

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

  • A. Mitra
  • Chemistry
    Acta crystallographica. Section F, Structural biology communications
  • 2019
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.

High-End Data Collection for Single-Particle Cryo-EM

  • F. Weis
  • Chemistry
    Microscopy and Microanalysis
  • 2019
Single-particle cryogenic transmission electron microscopy (cryo-EM) can be used to elucidate the 3D structure of macromolecular complexes. The sample is embedded in a thin layer of vitreous ice and

Cryo-electron microscopy reaches atomic resolution.

Cryo­EM is a decades-old structural­biology technique that has garnered increasing interest since around 2013 due to a series of techno­ logical and algorithmic advances that together drove a striking improvement in the resolution obtainable by this technique (described as the ‘resolution revolution’).

Biological Applications at the Cutting Edge of Cryo-Electron Microscopy

Developments in sample preparation methods and substrates, detectors, phase plates, and cryo-correlative light and electron microscopy that have contributed to this expansion are reviewed.

Recent Advances in Single Particle Cryo-electron Microscopy and Cryo-electron Tomography to Determine the Structures of Biological Macromolecules

  • M. Dutta
  • Chemistry
    Journal of the Indian Institute of Science
  • 2018
A detailed three-dimensional structure of macromolecular assemblies is necessary to understand their function which in turn helps to understand life. Cryo-electron microscopy (cryo-EM) is a powerful

Cryo-electron Microscopy Analysis of Structurally Heterogeneous Macromolecular Complexes

  • S. Jonić
  • Chemistry
    Computational and structural biotechnology journal
  • 2016

Atomic-resolution protein structure determination by cryo-EM.

A 1.25 Å-resolution structure of apoferritin is reported with a newly developed electron microscope that provides, to the authors' knowledge, unprecedented structural detail and a substantial improvement in the quality of the cryo-EM density map.

Cryo-EM is a powerful tool, but helical applications can have pitfalls.

The enormous potential for using cryo-EM, and also the pitfalls possible for helical assemblies when a near-atomic level of resolution is not reached are highlighted.

Cryo-Electron Tomography

An overview of recent advances in sample preparation, data acquisition and data processing is provided, including technology for focused ion beam milling, correlative light and electron microscopy, phase-plate imaging and direct electron detection, which show that these developments can be used synergistically to generate 3-D images of cells of unprecedented quality.

How cryo-EM is revolutionizing structural biology.




Electron counting and beam-induced motion correction enable near atomic resolution single particle cryoEM

This approach determined a 3.3-Å-resolution structure of an ∼700-kDa protein with D7 symmetry, the Thermoplasma acidophilum 20S proteasome, showing clear side-chain density and greatly enhances image quality and data acquisition efficiency.

Structure of the 30S ribosomal subunit

The crystal structure of the 30S subunit from Thermus thermophilus, refined to 3 Å resolution, is reported, which will facilitate the interpretation in molecular terms of lower resolution structural data on several functional states of the ribosome from electron microscopy and crystallography.

The complete atomic structure of the large ribosomal subunit at 2.4 A resolution.

The crystal structure of the large ribosomal subunit from Haloarcula marismortui is determined at 2.4 angstrom resolution, and it includes 2833 of the subunit's 3045 nucleotides and 27 of its 31 proteins.

Structure of the Yeast Mitochondrial Large Ribosomal Subunit

The structure of the yeast mitoribosomal large subunit is solved using single-particle cryo–electron microscopy and reveals a new exit tunnel path and architecture, unique elements of the E site, and a putative membrane docking site.

Age-dependent dissociation of ATP synthase dimers and loss of inner-membrane cristae in mitochondria

Electron cryotomography of whole mitochondria from the aging model organism Podospora anserina revealed profound age-dependent changes in membrane architecture, which would impair the ability of mitochondria to supply the cell with sufficient ATP to maintain essential cellular functions.

Electronic detectors for electron microscopy.

Structure of the TRPV1 ion channel determined by electron cryo-microscopy

Transient receptor potential (TRP) channels are sensors for a wide range of cellular and environmental signals, but elucidating how these channels respond to physical and chemical stimuli has been

Atomic model of the F420-reducing [NiFe] hydrogenase by electron cryo-microscopy using a direct electron detector

From the rigidity of the complex, it is concluded that catalysis is diffusion-limited and does not depend on protein flexibility or conformational changes.