ArticleNature methods2025
Dose-efficient cryo-electron microscopy for thick samples using tilt- corrected scanning transmission electron microscopy.
Article in Nature methods, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- FPGA-based scanner and SerialEM server for 4D-STEM electron tomography.Acta crystallographica. Section D, Structural biology · 2026Article
- Operando-Defined Amorphous Energy Materials for Electrochemical Energy Systems: From Structural Definition to Descriptor-Guided Design.Materials (Basel, Switzerland) · 2026Review
- Beyond structure: spectroscopic imaging in cryogenic electron microscopy.Current opinion in structural biology · 2026Review
- Contrast by electron microscopy in thick biological specimens.Journal of microscopy · 2025Article
- Defocus correction and noise reduction using a hybrid ptychography and Centre-of-Mass algorithm.Journal of microscopy · 2025Article
- Atomically resolved imaging of radiation-sensitive metal-organic frameworks via electron ptychography.Nature communications · 2025Article
- Low-dose cryo-electron ptychography of proteins at sub-nanometer resolution.Nature communications · 2024Article
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Authors and funding
13 authors.
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Abstract
Cryogenic electron microscopy is a powerful tool in structural biology. In thick specimens, challenges arise as an exponentially larger fraction of the transmitted electrons lose energy from inelastic scattering and can no longer be properly focused as a result of chromatic aberrations in the post-specimen optics. Rather than filtering out the inelastic scattering at the price of reducing potential signal, as is done in energy-filtered transmission electron microscopy, we show how a dose-efficient and unfiltered image can be rapidly obtained using tilt-corrected bright-field scanning transmission electron microscopy data collected on a pixelated detector. Enhanced contrast and a 3-5× improvement in dose efficiency are observed for two-dimensional images of intact bacterial cells and large organelles using tilt-corrected bright-field scanning transmission electron microscopy compared to energy-filtered transmission electron microscopy for thicknesses beyond 500 nm. As a proof of concept for the technique's performance in structural determination, we present a single-particle analysis map at sub-nanometer resolution for a highly symmetric virus-like particle determined from 789 particles.
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