ArticleInnovation (Cambridge (Mass.))2021
Determining structures in a native environment using single-particle cryoelectron microscopy images.
Article in Innovation (Cambridge (Mass.)), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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16 citing papers in PubMed, 25 citations in OpenAlex.
- CryoGO enables high-resolution structural profiling of endogenous cellular macromolecules.bioRxiv : the preprint server for biology · 2026Article
- Leopard-EM: an extensible 2D template-matching package to accelerate in situ structural biology.Acta crystallographica. Section D, Structural biology · 2026Article
- In situ structure of bacterial 50S ribosomes at 3.0 Å resolution from vitreous sections.Communications biology · 2025Article
- Cryo-EM single-particle analysis expanding towards increasingly native samples.Acta crystallographica. Section D, Structural biology · 2025Review
- Capturing eukaryotic ribosome dynamics in situ at high resolution.Nature structural & molecular biology · 2025Article
- Protein structure prediction via deep learning: an in-depth review.Frontiers in pharmacology · 2025Review
- Practical Guide for Implementing Cryogenic Electron Microscopy Structure Determination in Dermatology Research.The Journal of investigative dermatology · 2025Review
- In situ structural determination of cyanobacterial phycobilisome-PSII supercomplex by STAgSPA strategy.Nature communications · 2024Article
- Advances in cryo-ET data processing: meeting the demands of visual proteomics.Current opinion in structural biology · 2024Review
- Investigating the Balance between Structural Conservation and Functional Flexibility in Photosystem I.International journal of molecular sciences · 2024Review
- Article
- Cryo-EM structure of severe fever with thrombocytopenia syndrome virus.Nature communications · 2023Article
- Article
- Determining protein structures in cellular lamella at pseudo-atomic resolution by GisSPA.Nature communications · 2023Article
- Computational methods forFrontiers in cellular and infection microbiology · 2023Review
- CryomicroscopyFaraday discussions · 2022Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cryo-electron tomography is a powerful tool for structure determination in the native environment. However, this method requires the acquisition of tilt series, which is time-consuming and severely slows structure determination. By treating the densities of non-target protein as non-Gaussian noise, we developed a new target function that greatly improves the efficiency of recognizing the target protein in a single cryo-electron microscopy image. Moreover, we developed a sorting function that effectively eliminates the model dependence and improved the resolution during the subsequent structure refinement procedure. By eliminating model bias, our method allows using homolog proteins as models to recognize the target proteins in a complex context. Together, we developed an
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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.