ReviewMicroscopy (Oxford, England)2013
Problems in obtaining perfect images by single-particle electron cryomicroscopy of biological structures in amorphous ice.
Review in Microscopy (Oxford, England), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
28 citing papers in PubMed, 47 citations in OpenAlex.
- Laser phase plate improves structure determination of small proteins by cryo-EM.Science (New York, N.Y.) · 2026Article
- High-resolution cryo-EM using a common LaBScience advances · 2025Article
- Multi-species cryoEM calibration and workflow verification standard.Acta crystallographica. Section F, Structural biology communications · 2024Article
- Multi-species cryoEM calibration and workflow verification standard.bioRxiv : the preprint server for biology · 2024Article
- Structure determination by cryoEM at 100 keV.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Membranes under the Magnetic Lens: A Dive into the Diverse World of Membrane Protein Structures Using Cryo-EM.Chemical reviews · 2022Review
- Imaging biological macromolecules in thick specimens: The role of inelastic scattering in cryoEM.Ultramicroscopy · 2022Article
- Cryo-TEM simulations of amorphous radiation-sensitive samples using multislice wave propagation.IUCrJ · 2021Article
- A cryo-TSEM with temperature cycling capability allows deep sublimation of ice to uncover fine structures in thick cells.Scientific reports · 2021Article
- Article
- Electron Beam-Induced Transformation in High-Density Amorphous Ices.The journal of physical chemistry. B · 2020Article
- Present and Emerging Methodologies in Cryo-EM Single-Particle Analysis.Biophysical journal · 2020Review
- Sub-2 Angstrom resolution structure determination using single-particle cryo-EM at 200 keV.Journal of structural biology: X · 2020Article
- Macromolecule Particle Picking and Segmentation of a KLH Database by Unsupervised Cryo-EM Image Processing.Biomolecules · 2019Article
- Article
- Hands on Methods for High Resolution Cryo-Electron Microscopy Structures of Heterogeneous Macromolecular Complexes.Frontiers in molecular biosciences · 2019Review
- Processing apoferritin with the Appion pipeline.Journal of structural biology · 2018Article
- Structure of the apoptosome: mechanistic insights into activation of an initiator caspase from Drosophila.Genes & development · 2015Article
- Electron microscopy: Ultrastable gold substrates for electron cryomicroscopy.Science (New York, N.Y.) · 2014Article
- Single particle electron cryo-microscopy of a mammalian ion channel.Current opinion in structural biology · 2014Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Theoretical considerations together with simulations of single-particle electron cryomicroscopy images of biological assemblies in ice demonstrate that atomic structures should be obtainable from images of a few thousand asymmetric units, provided the molecular weight of the whole assembly being studied is greater than the minimum needed for accurate position and orientation determination. However, with present methods of specimen preparation and current microscope and detector technologies, many more particles are needed, and the alignment of smaller assemblies is difficult or impossible. Only larger structures, with enough signal to allow good orientation determination and with enough images to allow averaging of many hundreds of thousands or even millions of asymmetric units, have successfully produced high-resolution maps. In this review, we compare the contrast of experimental electron cryomicroscopy images of two smaller molecular assemblies, namely apoferritin and beta-galactosidase, with that expected from perfect simulated images calculated from their known X-ray structures. We show that the contrast and signal-to-noise ratio of experimental images still require significant improvement before it will be possible to realize the full potential of single-particle electron cryomicroscopy. In particular, although reasonably good orientations can be obtained for beta-galactosidase, we have been unable to obtain reliable orientation determination from experimental images of apoferritin. Simulations suggest that at least 2-fold improvement of the contrast in experimental images at ~10 Å resolution is needed and should be possible.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.