ArticleScientific reports2021
Below 3 Å structure of apoferritin using a multipurpose TEM with a side entry cryoholder.
Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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Who cites it
10 citing papers in PubMed, 15 citations in OpenAlex.
- Article
- Atomic resolution cryo-EM at 200 keV.IUCrJ · 2026Article
- The Role of Confinement in Biomineralization.Chemical reviews · 2025Review
- Unravelling complex mechanisms in materials processes with cryogenic electron microscopy.Chemical science · 2025Review
- Revisiting sodium phosphotungstate and ammonium molybdate as nonradioactive negative-staining agents for single-particle analysis.Acta crystallographica. Section F, Structural biology communications · 2024Article
- Small extracellular vesicles in follicular fluids for predicting reproductive outcomes in assisted reproductive technology.Communications medicine · 2024Article
- Overcoming resolution loss due to thermal magnetic field fluctuations from phase plates in transmission electron microscopy.Ultramicroscopy · 2023Article
- Overcoming resolution loss due to thermal magnetic field fluctuations from phase plates in transmission electron microscopy.bioRxiv : the preprint server for biology · 2023Article
- Microsecond melting and revitrification of cryo samples: protein structure and beam-induced motion.Acta crystallographica. Section D, Structural biology · 2022Article
- Sub-3 Å Cryo-EM Structures of Necrosis Virus Particles via the Use of Multipurpose TEM with Electron Counting Camera.International journal of molecular sciences · 2021Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Recently, the structural analysis of protein complexes by cryo-electron microscopy (cryo-EM) single particle analysis (SPA) has had great impact as a biophysical method. Many results of cryo-EM SPA are based on data acquired on state-of-the-art cryo-electron microscopes customized for SPA. These are currently only available in limited locations around the world, where securing machine time is highly competitive. One potential solution for this time-competitive situation is to reuse existing multi-purpose equipment, although this comes with performance limitations. Here, a multi-purpose TEM with a side entry cryo-holder was used to evaluate the potential of high-resolution SPA, resulting in a 3 Å resolution map of apoferritin with local resolution extending to 2.6 Å. This map clearly showed two positions of an aromatic side chain. Further, examination of optimal imaging conditions depending on two different multi-purpose electron microscope and camera combinations was carried out, demonstrating that higher magnifications are not always necessary or desirable. Since automation is effectively a requirement for large-scale data collection, and augmenting the multi-purpose equipment is possible, we expanded testing by acquiring data with SerialEM using a β-galactosidase test sample. This study demonstrates the possibilities of more widely available and established electron microscopes, and their applications for cryo-EM SPA.
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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.