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Achieving better-than-3-Å resolution by single-particle cryo-EM at 200 keV

https://doi.org/10.1038/nmeth.4461
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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1007/s007920000171openalex-snapshot
Probing stability–activity relationships in the thermophilic proteasome from Thermoplasma acidophilum by random mutagenesis
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inferredcites →https://doi.org/10.1016/j.jsb.2006.05.009openalex-snapshot
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inferredcites →https://doi.org/10.1016/j.jsb.2006.07.003openalex-snapshot
SPARX, a new environment for Cryo-EM image processing
inferredcites →https://doi.org/10.1016/j.jsb.2009.01.002openalex-snapshot
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inferredcites →https://doi.org/10.1016/j.jsb.2009.01.004openalex-snapshot
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inferredcites →https://doi.org/10.1016/j.jsb.2010.12.005openalex-snapshot
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inferredcites →https://doi.org/10.1016/j.jsb.2012.09.006openalex-snapshot
RELION: Implementation of a Bayesian approach to cryo-EM structure determination
inferredcites →https://doi.org/10.1016/j.jsb.2013.08.002openalex-snapshot
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inferredcites →https://doi.org/10.1016/j.jsb.2014.09.008openalex-snapshot
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inferredcites →https://doi.org/10.1016/j.jsb.2015.08.007openalex-snapshot
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inferredcites →https://doi.org/10.1016/j.jsb.2015.08.008openalex-snapshot
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inferredcites →https://doi.org/10.1016/j.str.2018.10.003openalex-snapshot
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inferredcites →https://doi.org/10.1016/j.ultramic.2013.06.004openalex-snapshot
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inferredcites →https://doi.org/10.1016/j.ultramic.2014.08.002openalex-snapshot
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inferredcites →https://doi.org/10.1038/nature12104openalex-snapshot
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inferredcites →https://doi.org/10.1038/nature19948openalex-snapshot
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inferredcites →https://doi.org/10.1038/ncomms16099openalex-snapshot
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inferredcites →https://doi.org/10.1038/nmeth.2115openalex-snapshot
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inferredcites →https://doi.org/10.1038/nmeth.2472openalex-snapshot
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inferredcites →https://doi.org/10.1038/nmeth.3541openalex-snapshot
EMRinger: side chain–directed model and map validation for 3D cryo-electron microscopy
inferredcites →https://doi.org/10.1038/nmeth.4169openalex-snapshot
cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination
inferredcites →https://doi.org/10.1038/nmeth.4193openalex-snapshot
MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy
inferredcites →https://doi.org/10.1038/nprot.2007.474openalex-snapshot
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inferredcites →https://doi.org/10.1038/protex.2017.108openalex-snapshot
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inferredcites →https://doi.org/10.1093/nar/gkh131openalex-snapshot
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inferredcites →https://doi.org/10.1093/nar/gkh151openalex-snapshot
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inferredcites →https://doi.org/10.1107/97809553602060000865openalex-snapshot
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inferredcites →https://doi.org/10.1107/s0907444909042073openalex-snapshot
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inferredcites →https://doi.org/10.1107/s0907444909052925openalex-snapshot
PHENIX : a comprehensive Python-based system for macromolecular structure solution
inferredcites →https://doi.org/10.1126/science.1259530openalex-snapshot
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inferredcites →https://doi.org/10.1126/science.aac5789openalex-snapshot
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inferredcites →https://doi.org/10.1128/jvi.03402-13openalex-snapshot
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inferredcites →https://doi.org/10.2210/pdb5ni1/pdbopenalex-snapshot
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inferredcites →https://doi.org/10.5772/61781openalex-snapshot
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inferredcites →https://doi.org/10.7554/elife.03665openalex-snapshot
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inferredcites →https://doi.org/10.7554/elife.06380openalex-snapshot
2.8 Å resolution reconstruction of the Thermoplasma acidophilum 20S proteasome using cryo-electron microscopy
inferredcites →https://doi.org/10.7554/elife.06980openalex-snapshot
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inferredcites →https://doi.org/10.7554/elife.13046openalex-snapshot
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inferredcites →https://doi.org/10.7554/elife.17219openalex-snapshot
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inferredcites →https://doi.org/10.7554/elife.18722openalex-snapshot
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inferredcites →https://doi.org/10.7554/elife.23006openalex-snapshot
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What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

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Structure of the RhlR-PqsE Complex From Pseudomonas aeruginosa Reveals a New Mechanism of Quorum Sensing Transcriptional Regulation
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Cryo‐Electron Microscopy in Drug Discovery and Development: Opportunities and Challenges
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The Evolving Role of Structural Biology in Drug Discovery
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The Influence of Detector Quality and Throughput for Cryo-EM of Challenging Proteins
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Expanding the Dimensions of a Small, Two-Dimensional Diffraction Detector
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First Results from a Novel CMOS Detector Optimised for 100keV CryoEM
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Benchmarking Cryo-EM Single Particle Analysis Workflows at CEMRC
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Sub-2 Å Ewald curvature corrected structure of an AAV2 capsid variant
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High-resolution structure determination of sub-100 kDa complexes using conventional cryo-EM
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Structure of the SARS-CoV nsp12 polymerase bound to nsp7 and nsp8 co-factors
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Single particle cryo-EM reconstruction of 52 kDa streptavidin at 3.2 Angstrom resolution
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Robust ultraclean atomically thin membranes for atomic-resolution electron microscopy
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Structure and dynamics of the ASB9 CUL-RING E3 Ligase
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Structures of the human LONP1 protease reveal regulatory steps involved in protease activation
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Structural basis for Rab6 activation by the Ric1-Rgp1 complex
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Cryo-EM structures of human ClpXP reveal mechanisms of assembly and proteolytic activation
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A metabolite-bridged complex between SerRS and SIRT2 couples NAD⁺ metabolism to translation control
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Membrane protein structure and dynamics probed by MicroED
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Proteolytic systems of archaea: slicing, dicing, and mincing in the extreme
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Structures of multisubunit membrane complexes with the CRYO ARM 200
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The Engines of Discovery: How Cryo-EM Technology Transformed Biology
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Sub-3 Å resolution structure of apoferritin using a multi-purpose TEM with a side-entry cryo-holder
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Size matters: optimal mask diameter and box size for single-particle cryogenic electron microscopy
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Optimized cryo-EM data acquisition workflow by sample thickness determination
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Uncovering Protein Ensembles: Automated Multiconformer Model Building for X-ray Crystallography and Cryo-EM
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Single particle cryo-electron microscopy with an enhanced 200 kV cryo-TEM configuration achieves near-atomic resolution
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Distinct Structural Features of the Lon Protease Drive Conserved Hand-over-Hand Substrate Translocation
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CryoEM at 100 keV: a demonstration and prospects
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Throughput and resolution with a next-generation direct electron detector
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A potential difference for single-particle cryo-EM
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Estimation of high-order aberrations and anisotropic magnification from cryo-EM data sets in RELION -3.1
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High-resolution cryo-EM reconstructions in the presence of substantial aberrations
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High-resolution cryo-EM using beam-image shift at 200 keV
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High-speed high-resolution data collection on a 200 keV cryo-TEM
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Atomic resolution cryo-EM at 200 keV
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inferred← citeshttps://doi.org/10.1107/s2053230x19004424openalex-snapshot
Cryo-EM structure of the Ebola virus nucleoprotein–RNA complex
inferred← citeshttps://doi.org/10.1107/s2053230x20000308openalex-snapshot
Structure of the AAVhu.37 capsid by cryoelectron microscopy
inferred← citeshttps://doi.org/10.1107/s2059798321001935openalex-snapshot
Cryo-EM of kinesin-binding protein: challenges and opportunities from protein-surface interactions
inferred← citeshttps://doi.org/10.1107/s205979832100334xopenalex-snapshot
Optimized cryo-EM data-acquisition workflow by sample-thickness determination
inferred← citeshttps://doi.org/10.1107/s2059798321012110openalex-snapshot
A case for glycerol as an acceptable additive for single-particle cryoEM samples
inferred← citeshttps://doi.org/10.1107/s205979832101216xopenalex-snapshot
CryoEM analysis of small plant biocatalysts at sub-2 Å resolution
inferred← citeshttps://doi.org/10.1111/jmi.12834openalex-snapshot
Current outcomes when optimizing ‘standard’ sample preparation for single‐particle cryo‐EM
inferred← citeshttps://doi.org/10.1111/mmi.14637openalex-snapshot
CryoEM of bacterial secretion systems: A primer for microbiologists
inferred← citeshttps://doi.org/10.1126/sciadv.aba8404openalex-snapshot
Structural basis for distinct operational modes and protease activation in AAA+ protease Lon
inferred← citeshttps://doi.org/10.1126/sciadv.aeh5900openalex-snapshot
Acoustofluidic cryo-EM enables in situ particle manipulation for uniform, high-quality cryo-EM specimens
inferred← citeshttps://doi.org/10.1126/science.aar4056openalex-snapshot
Cryo-EM structure of a mitochondrial calcium uniporter
inferred← citeshttps://doi.org/10.1126/science.aeh0665openalex-snapshot
Laser phase plate improves structure determination of small proteins by cryo-EM
inferred← citeshttps://doi.org/10.1146/annurev-biochem-072020-020231openalex-snapshot
Preparing Better Samples for Cryo–Electron Microscopy: Biochemical Challenges Do Not End with Isolation and Purification
inferred← citeshttps://doi.org/10.1146/annurev-biochem-081720-020121openalex-snapshot
An Overview of Microcrystal Electron Diffraction (MicroED)
inferred← citeshttps://doi.org/10.1146/annurev-biophys-070317-032828openalex-snapshot
How Good Can Single-Particle Cryo-EM Become? What Remains Before It Approaches Its Physical Limits?
inferred← citeshttps://doi.org/10.1186/s12859-019-2926-yopenalex-snapshot
AutoCryoPicker: an unsupervised learning approach for fully automated single particle picking in Cryo-EM images
inferred← citeshttps://doi.org/10.1186/s12859-020-03809-7openalex-snapshot
DeepCryoPicker: fully automated deep neural network for single protein particle picking in cryo-EM
inferred← citeshttps://doi.org/10.1186/s44330-025-00047-2openalex-snapshot
In situ structural analysis of mammalian cells using a 200 kV electron cryomicroscope – implications for research infrastructure
inferred← citeshttps://doi.org/10.12688/f1000research.25097.1openalex-snapshot
Advances in methods for atomic resolution macromolecular structure determination
inferred← citeshttps://doi.org/10.1371/journal.pone.0232540openalex-snapshot
2.7 Å cryo-EM structure of vitrified M. musculus H-chain apoferritin from a compact 200 keV cryo-microscope
inferred← citeshttps://doi.org/10.1515/hsz-2019-0344openalex-snapshot
Proteasomes: unfoldase-assisted protein degradation machines
inferred← citeshttps://doi.org/10.1515/mim-2025-0039openalex-snapshot
A cost-effective 200 kV cryo-EM core facility for high resolution single particle analysis
inferred← citeshttps://doi.org/10.17169/refubium-33042openalex-snapshot
CryoEM analysis of small plant biocatalysts at sub-2 Å resolution
inferred← citeshttps://doi.org/10.32469/10355/79558openalex-snapshot
Fully automated deep supervised and unsupervised learning approaches for 3D protein cryo-EM density map reconstruction
inferred← citeshttps://doi.org/10.32604/cmc.2022.025072openalex-snapshot
Urdnet: A Cryo-EM Particle Automatic Picking Method
inferred← citeshttps://doi.org/10.3389/fmolb.2018.00050openalex-snapshot
Benchmarking cryo-EM Single Particle Analysis Workflow
inferred← citeshttps://doi.org/10.3389/fmolb.2024.1404885openalex-snapshot
Machine learning approaches to cryoEM density modification differentially affect biomacromolecule and ligand density quality
inferred← citeshttps://doi.org/10.3390/genes10090666openalex-snapshot
A Super-Clustering Approach for Fully Automated Single Particle Picking in Cryo-EM
inferred← citeshttps://doi.org/10.3390/molecules25010082openalex-snapshot
Advances in Structure Modeling Methods for Cryo-Electron Microscopy Maps
inferred← citeshttps://doi.org/10.3390/vaccines9030301openalex-snapshot
Vaccine Efficacy of Self-Assembled Multimeric Protein Scaffold Particles Displaying the Glycoprotein Gn Head Domain of Rift Valley Fever Virus
inferred← citeshttps://doi.org/10.5940/jcrsj.61.43openalex-snapshot
Observation of Hydrated Proteins and Cells by Electron Cryo-Microscopy
inferred← citeshttps://doi.org/10.64898/2026.03.17.712260openalex-snapshot
A Surfactant Cocktail Overcomes Air-Water Interface Artifacts in Single-Particle CryoEM
inferred← citeshttps://doi.org/10.64898/2026.04.16.718662openalex-snapshot
cryoAgent: An agentic workflow for robust and adaptive end-to-end cryo-EM image processing
inferred← citeshttps://doi.org/10.7554/elife.43542openalex-snapshot
Automated cryo-EM structure refinement using correlation-driven molecular dynamics
inferred← citeshttps://doi.org/10.7554/elife.50003openalex-snapshot
A structural mechanism for phosphorylation-dependent inactivation of the AP2 complex
inferred← citeshttps://doi.org/10.7554/elife.79676openalex-snapshot
The Nse5/6-like SIMC1-SLF2 complex localizes SMC5/6 to viral replication centers
inferred← citeshttps://doi.org/10.7554/elife.90606openalex-snapshot
Automated multiconformer model building for X-ray crystallography and cryo-EM
inferred← citeshttps://doi.org/10.7554/elife.90606.1openalex-snapshot
Uncovering Protein Ensembles: Automated Multiconformer Model Building for X-ray Crystallography and Cryo-EM
inferred← citeshttps://doi.org/10.7554/elife.90606.2openalex-snapshot
Uncovering Protein Ensembles: Automated Multiconformer Model Building for X- ray Crystallography and Cryo-EM
inferred← citeshttps://doi.org/10.7554/elife.90606.3openalex-snapshot
Automated multiconformer model building for X-ray crystallography and cryo-EM
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