The Resolution Revolution

RELION: Implementation of a Bayesian approach to cryo-EM structure determination

Scheres, S. H. W. (2012) · Journal of Structural Biology · doi:10.1016/j.jsb.2012.09.006 · Cited by 5,446

The Complete Atomic Structure of the Large Ribosomal Subunit at 2.4 Å Resolution

Ban, N., Nissen, P., Hansen, J., Moore, P. B., & Steitz, T. A. (2000) · Science · doi:10.1126/science.289.5481.905 · Cited by 3,327

Structure of the 30S ribosomal subunit

Wimberly, B. T., Brodersen, D. E., Clemons, W. M., Morgan-Warren, R. J., Carter, A. P., Vonrhein, C., Hartsch, T., & Ramakrishnan, V. (2000) · Nature · doi:10.1038/35030006 · Cited by 2,035

Electron counting and beam-induced motion correction enable near atomic resolution single particle cryoEM

Li, X.-M., Mooney, P., Zheng, S., Booth, C., Braunfeld, M. B., Gubbens, S., Agard, D., & Cheng, Y.-F. (2013) · Nature Methods · doi:10.1038/nmeth.2472 · Cited by 1,866

Structure of the TRPV1 ion channel determined by electron cryo-microscopy

Liao, M., Cao, E., Julius, D. J., & Cheng, Y. (2013) · Nature · doi:10.1038/nature12822 · Cited by 1,731

Structure of the Yeast Mitochondrial Large Ribosomal Subunit

Amunts, A., Brown, A., Bai, X., Llacer, J. L., Hussain, T., Emsley, P., Long, F., Murshudov, G. N., Scheres, S. H. W., & Ramakrishnan, V. (2014) · Science · doi:10.1126/science.1249410 · Cited by 580

Age-dependent dissociation of ATP synthase dimers and loss of inner-membrane cristae in mitochondria

Daum, B., Walter, A., Horst, A., Osiewacz, H. D., & Kühlbrandt, W. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1305462110 · Cited by 229

Electronic detectors for electron microscopy

Faruqi, A. R., & Henderson, R. A. (2007) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2007.08.014 · Cited by 138

Atomic model of the F420-reducing [NiFe] hydrogenase by electron cryo-microscopy using a direct electron detector

Allegretti, M., Mills, D. J., McMullan, G., Kühlbrandt, W., & Vonck, J. (2014) · eLife · doi:10.7554/elife.01963 · Cited by 138

Determination of protein structure at 8.5 Å resolution using cryo-electron tomography and sub-tomogram averaging

Schur, F. K. M., Hagen, W. J. H., de Marco, A., & Briggs, J. A. G. (2013) · Journal of Structural Biology · doi:10.1016/j.jsb.2013.10.015 · Cited by 90

Following Natures Lead: On the Construction of Membrane-Inserted Toxins in Lipid Bilayer Nanodiscs

Akkaladevi, N., Mukherjee, S., Katayama, H., Janowiak, B. E., Patel, D. K., Gogol, E. P., Pentelute, B. L., Collier, R. J., & Fisher, M. T. (2015) · The Journal of Membrane Biology · doi:10.1007/s00232-014-9768-3 · Cited by 14

Near-atomic resolution reconstructions using a mid-range electron microscope operated at 200kV

Campbell, M. G., Kearney, B. M., Cheng, A., Potter, C. S., Johnson, J. E., Carragher, B. O., & Veesler, D. (2014) · Journal of Structural Biology · doi:10.1016/j.jsb.2014.09.008 · Cited by 14

Modular Polyketide Synthases (PKSs): A New Model Fits All?

Rittner, A., & Grininger, M. (2014) · ChemBioChem · doi:10.1002/cbic.201402432 · Cited by 14

Measurement of local resolution in electron tomography

Vilas, J. L., Otón, J., Messaoudi, C., Melero, R., Conesa, P., Ramírez-Aportela, E., Mota, J., Martínez, M., Jimenez, A., Marabini, R., et al. (2019) · Journal of Structural Biology X · doi:10.1016/j.yjsbx.2019.100016 · Cited by 14

Toward a Systematic Structural and Functional Annotation of Solute Carriers Transporters—Example of the SLC6 and SLC7 Families

Colas, C. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.01229 · Cited by 15

Pre-pro is a fast pre-processor for single-particle cryo-EM by enhancing 2D classification

Chung, S.-C., Lin, H., Niu, P.-Y., Huang, S.-H., Tu, I., & Chang, W. (2020) · Communications Biology · doi:10.1038/s42003-020-01229-0 · Cited by 14

Structural basis of the (in)activity of the apical DNA damage response kinases ATM, ATR and DNA-PKcs

Jansma, M., & Hopfner, K. (2020) · Progress in Biophysics and Molecular Biology · doi:10.1016/j.pbiomolbio.2020.10.009 · Cited by 14

Endocytosed nanogold fiducials for improved in-situ cryo–electron tomography tilt-series alignment

Berger, C., Ravelli, R. B. G., López‐Iglesias, C., & Peters, P. J. (2021) · Journal of Structural Biology · doi:10.1016/j.jsb.2021.107698 · Cited by 14

ScanNet: A Web Server for Structure-based Prediction of Protein Binding Sites with Geometric Deep Learning

Tubiana, J., Schneidman‐Duhovny, D., & Wolfson, H. J. (2022) · Journal of Molecular Biology · doi:10.1016/j.jmb.2022.167758 · Cited by 15

Integration of an Event-driven Timepix3 Hybrid Pixel Detector into a Cryo-EM Workflow

van Schayck, J. P., Zhang, Y., Knoops, K., Peters, P. J., & Ravelli, R. B. G. (2022) · Microscopy and Microanalysis · doi:10.1093/micmic/ozac009 · Cited by 14

Below 3 Å structure of apoferritin using a multipurpose TEM with a side entry cryoholder

Kayama, Y., Burton‐Smith, R. N., Song, C., Terahara, N., Kato, T., & Murata, K. (2021) · Scientific Reports · doi:10.1038/s41598-021-87183-1 · Cited by 14

Cryo-EM Analyses Permit Visualization of Structural Polymorphism of Biological Macromolecules

Chang, W., Huang, S.-H., Lin, H., Chung, S.-C., & Tu, I. (2021) · Frontiers in Bioinformatics · doi:10.3389/fbinf.2021.788308 · Cited by 13

Progress in spatial resolution of structural analysis by cryo-EM

Fukuda, Y., Stapleton, K., & Kato, T. (2022) · Microscopy · doi:10.1093/jmicro/dfac053 · Cited by 13

Integrating model simulation tools and cryo‐electron microscopy

Beton, J. G., Cragnolini, T., Kaleel, M., Mulvaney, T., Sweeney, A., & Topf, M. (2022) · Wiley Interdisciplinary Reviews Computational Molecular Science · doi:10.1002/wcms.1642 · Cited by 11

Predictive modeling and cryo-EM: A synergistic approach to modeling macromolecular structure

Corum, M. R., Venkannagari, H., Hryc, C. F., & Baker, M. L. (2024) · Biophysical Journal · doi:10.1016/j.bpj.2024.01.021 · Cited by 15

High-resolution cryo-EM using a common LaB 6 120-keV electron microscope equipped with a sub–200-keV direct electron detector

Venugopal, H., Mobbs, J. I., Taveneau, C., Fox, D., Vuckovic, Z., Gulati, S., Knott, G. J., Grinter, R., Thal, D. M., Mick, S. E., et al. (2025) · Science Advances · doi:10.1126/sciadv.adr0438 · Cited by 13

Extending the reach of single-particle cryoEM

Patwardhan, A., Henderson, R. A., & Russo, C. J. (2025) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2025.103005 · Cited by 14

High-resolution cryo-EM proteasome structures in drug development

Morris, E. P., & da Fonseca, P. C. A. (2017) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798317007021 · Cited by 13

Structural basis of reiterative transcription from the pyrG and pyrBI promoters by bacterial RNA polymerase

Shin, Y., Hedglin, M., & Murakami, K. (2019) · bioRxiv · doi:10.1093/nar/gkz1221 · Cited by 12

Wielding the power of interactive molecular simulations

Lanrezac, A., Férey, N., & Baaden, M. (2021) · Wiley Interdisciplinary Reviews Computational Molecular Science · doi:10.1002/wcms.1594 · Cited by 14

Finding Nano-Ötzi: Cryo-Electron Tomography Visualization Guided by Learned Segmentation

Nguyen, N., Bohak, C., Engel, D., Mindek, P., Strnad, O., Wonka, P., Li, S., Ropinski, T., & Viola, I. (2022) · IEEE Transactions on Visualization and Computer Graphics · doi:10.1109/tvcg.2022.3186146 · Cited by 13

Ribosome Rescue and Protein Quality Control in Concert

Hilal, T., & Spahn, C. M. T. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.01.029 · Cited by 13

Rational Design of Proteasome Inhibitors as Antimalarial Drugs

Chapelain, C. L., & Groll, M. (2016) · Angewandte Chemie International Edition · doi:10.1002/anie.201602519 · Cited by 13

Structures of enveloped virions determined by cryogenic electron microscopy and tomography

Stass, R., Ng, W. M., Kim, Y. C., & Huiskonen, J. T. (2019) · Advances in virus research · doi:10.1016/bs.aivir.2019.07.009 · Cited by 15

Stages, scaffolds and strings in the spatial organisation of non-homologous end joining: Insights from X-ray diffraction and Cryo-EM

Liang, S., Chaplin, A. K., Stavridi, A. K., Appleby, R. E., Hnízda, A., & Blundell, T. L. (2020) · Progress in Biophysics and Molecular Biology · doi:10.1016/j.pbiomolbio.2020.11.008 · Cited by 13

Travel light: Essential packing for membrane proteins with an active lifestyle

Johansen, N. T., Tidemand, F. G., Pedersen, M. C., & Arleth, L. (2022) · Biochimie · doi:10.1016/j.biochi.2022.07.014 · Cited by 13

Cryo-EM structures of apo-APC/C and APC/CCDH1:EMI1 complexes provide insights into APC/C regulation

Höfler, A., Yu, J., Yang, J., Zhang, Z., Chang, L., McLaughlin, S. H., Grime, G. W., Garman, E. F., Boland, A., & Barford, D. (2024) · Nature Communications · doi:10.1038/s41467-024-54398-5 · Cited by 18

Unfreezing structural biology for drug discovery

Stachowski, T. R., & Fischer, M. M. (2025) · Nature Chemical Biology · doi:10.1038/s41589-025-02047-3 · Cited by 14

AAnchor: CNN guided detection of anchor amino acids in high resolution cryo-EM density maps

Rozanov, M., & Wolfson, H. J. (2018) · IEEE International Conference on Bioinformatics and Biomedicine (BIBM) · doi:10.1109/bibm.2018.8621288 · Cited by 12

Chasing Tails: Cathepsin-L Improves Structural Analysis of Histones by HX-MS*[S]

Papanastasiou, M., Mullahoo, J., DeRuff, K. C., Bajrami, B., Karageorgos, I. L., Johnston, S. E., Peckner, R., Myers, S. A., Carr, S. A., & Jaffe, J. D. (2019) · Molecular & Cellular Proteomics · doi:10.1074/mcp.ra119.001325 · Cited by 12

Cryo-EM structure-based selection of computed ligand poses enables design of MTA-synergic PRMT5 inhibitors of better potency

Zhou, W., Yadav, G. P., Yang, X. T., Qin, F., Li, C., & Jiang, Q. (2022) · Communications Biology · doi:10.1038/s42003-022-03991-9 · Cited by 13

Future opportunities in solute carrier structural biology

Newstead, S. L. (2024) · Nature Structural & Molecular Biology · doi:10.1038/s41594-024-01271-0 · Cited by 12

Delineating organizational principles of the endogenous L-A virus by cryo-EM and computational analysis of native cell extracts

Schmidt, L., Tüting, C., Kyrilis, F. L., Hamdi, F., Semchonok, D. A., Hause, G., Meister, A., Ihling, C. H., Shah, P. N. M., Stubbs, M. T., et al. (2024) · Communications Biology · doi:10.1038/s42003-024-06204-7 · Cited by 14

Impact of structural biology and the protein data bank on us fda new drug approvals of low molecular weight antineoplastic agents 2019–2023

Burley, S. K., Wu-Wu, A., Dutta, S., Ganesan, S., & Zheng, X. F. S. (2024) · Oncogene · doi:10.1038/s41388-024-03077-2 · Cited by 14

Automated fiducial-based alignment of cryo-electron tomography tilt series in Dynamo

Coray, R., Navarro, P. P., Scaramuzza, S., Stahlberg, H., & Castaño‐Díez, D. (2024) · Structure · doi:10.1016/j.str.2024.07.003 · Cited by 12

A new age in structural S-layer biology: Experimental and in silico milestones

Grill-Walcher, S., & Schäffer, C. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.110205 · Cited by 12

Ensemble refinement of mismodeled cryo-EM RNA structures using all-atom simulations

Posani, E., Janoš, P., Haack, D. B., Toor, N., Bonomi, M., Magistrato, A., & Bussi, G. (2025) · Nature Communications · doi:10.1038/s41467-025-59769-0 · Cited by 16

Sub-3 Å resolution protein structure determination by single-particle cryo-EM at 100 keV

Karia, D., Koh, F., Yang, W., Cushing, V. I., Basanta, B., Mihaylov, D. B., Khavnekar, S., Vyroubal, O., Malínský, M., Sháněl, O., et al. (2025) · Structure · doi:10.1016/j.str.2025.07.007 · Cited by 12

Variability of Protein Structure Models from Electron Microscopy

Monroe, L. K., Terashi, G., & Kihara, D. (2017) · Structure · doi:10.1016/j.str.2017.02.004 · Cited by 12

Single particle cryo-EM — an optimal tool to study cytoskeletal proteins

Pospich, S., & Raunser, S. (2018) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2018.07.006 · Cited by 12

Beyond history and “on a roll”: The list of the most well‐studied human protein structures and overall trends in the protein data bank

Li, Z., & Buck, M. (2021) · Protein Science · doi:10.1002/pro.4038 · Cited by 16

CryoEM of bacterial secretion systems: A primer for microbiologists

Umrekar, T. R., Cohen, E. J., Drobnič, T., González-Rodríguez, N., & Beeby, M. (2020) · Molecular Microbiology · doi:10.1111/mmi.14637 · Cited by 12

Capturing actin assemblies in cells using in situ cryo-electron tomography

Schneider, J., & Jasnin, M. (2022) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2022.151224 · Cited by 12

CryoEM of Viral Ribonucleoproteins and Nucleocapsids of Single-Stranded RNA Viruses

Modrego, A., Carlero, D., Arranz, R., & Martín‐Benito, J. (2023) · Viruses · doi:10.3390/v15030653 · Cited by 12

Virus Structures by X-Ray Free-Electron Lasers

Meents, A., & Wiedorn, M. O. (2019) · Annual Review of Virology · doi:10.1146/annurev-virology-092818-015724 · Cited by 12

Seeing Atoms: Single-Particle Cryo-EM Breaks the Atomic Barrier

Tan, Y. Z., & Carragher, B. O. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.11.043 · Cited by 12

Bayesian inference of rotor ring stoichiometry from electron microscopy images of archaeal ATP synthase

Cossio, P., Allegretti, M., Mayer, F., Müller, V., Vonck, J., & Hummer, G. (2018) · Microscopy · doi:10.1093/jmicro/dfy033 · Cited by 12

Structural biology in the age of X-ray free-electron lasers and exascale computing

Mous, S. T., Poitevin, F., Hunter, M. S., Asthagiri, D. N., & Beck, T. L. (2024) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2024.102808 · Cited by 13

Cryo-electron microscopy in the study of virus entry and infection

Dutta, M., & Acharya, P. (2024) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2024.1429180 · Cited by 12

The chemistry of electrical signaling in sodium channels from bacteria and beyond

Catterall, W. A., El-Din, T. M. G., & Wisedchaisri, G. (2024) · Cell chemical biology · doi:10.1016/j.chembiol.2024.07.010 · Cited by 11

Quantum mechanics paradox in protein structure prediction: Intrinsically linked to sequence yet independent of it

Niazi, S. K. (2025) · Computational and Structural Biotechnology Reports · doi:10.1016/j.csbr.2025.100039 · Cited by 12

Disulfide-constrained Fabs overcome target size limitation for high-resolution single particle cryoEM

Kung, J. E., Johnson, M. C., Tegunov, D., Jao, C. C., Wu, P., Oh, A., Lin, M. H., Daria, J. M., Koth, C. M., Arthur, C. P., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-63766-8 · Cited by 11

The Electron Microscopy eXchange (EMX) initiative

Marabini, R., Ludtke, S. J., Murray, S. C., Chiu, W., de la Rosa-Trevin, J. M., Patwardhan, A., Heymann, J. B., & Carazo, J. M. (2016) · Journal of Structural Biology · doi:10.1016/j.jsb.2016.02.008 · Cited by 11

Recent progress in structure and dynamics of dual-membrane-spanning bacterial nanomachines

Gold, V. A. M., & Kudryashev, M. (2016) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2016.03.001 · Cited by 12

Structural biology data archiving – where we are and what lies ahead

Kleywegt, G. J., Velankar, S. S., & Patwardhan, A. (2018) · FEBS Letters · doi:10.1002/1873-3468.13086 · Cited by 11

Single-particle cryo-EM: beyond the resolution

Armache, J., & Cheng, Y. (2019) · National Science Review · doi:10.1093/nsr/nwz127 · Cited by 11

Supervised Regression Study for Electron Microscopy Data

Al-Haija, Q. S. A., & Nasr, K. A. (2019) · IEEE International Conference on Bioinformatics and Biomedicine (BIBM) · doi:10.1109/bibm47256.2019.8983101 · Cited by 11

Cryo-electron structures of the extreme thermostable enzymes Sulfur Oxygenase Reductase and Lumazine Synthase

Sobhy, M. A., Zhao, L., Anjum, D. H., Behzad, A. R., Takahashi, M., Tehseen, M., Biasio, A. D., Sougrat, R., & Hamdan, S. M. (2022) · PLoS ONE · doi:10.1371/journal.pone.0275487 · Cited by 11

Mahalanobis distance for class averaging of cryo-EM images

Bhamre, T., Zhao, Z., & Singer, A. (2017) · IEEE International Symposium on Biomedical Imaging (ISBI) · doi:10.1109/isbi.2017.7950605 · Cited by 11

In Situ Imaging and Structure Determination of Bacterial Toxin Delivery Systems Using Electron Cryotomography

Ghosal, D., Kaplan, M., Chang, Y., & Jensen, G. J. (2019) · Methods in molecular biology · doi:10.1007/978-1-4939-9048-1_16 · Cited by 11

Visualizing hazardous solids with cryogenic electron microscopy (Cryo-EM)

Gong, Y., Gu, T., Ling, L., Qiu, R., & Zhang, W. (2022) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2022.129192 · Cited by 11

AlphaFold and the future of structural biology

Read, R. J., Baker, E. N., Bond, C. S., Garman, E. F., & van Raaij, M. J. (2023) · IUCrJ · doi:10.1107/s2052252523004943 · Cited by 12

AlphaFold and the future of structural biology

Read, R. J., Baker, E. N., Bond, C. S., Garman, E. F., & van Raaij, M. J. (2023) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798323004928 · Cited by 12

Advances in Peptide/Protein Structure Prediction Tools and their Relevance for Structural Biology in the Last Decade

de Rezende, S. B., de Lima, L. R., Macedo, M. L. R., Franco, O. L., & Cardoso, M. H. E. S. (2023) · Current Bioinformatics · doi:10.2174/1574893618666230412080702 · Cited by 10

M-Denoiser: Unsupervised image denoising for real-world optical and electron microscopy data

Chong, X., Cheng, M., Fan, W., Li, Q., & Leung, H. W. H. (2023) · Computers in Biology and Medicine · doi:10.1016/j.compbiomed.2023.107308 · Cited by 10

Virus structures revealed by advanced cryoelectron microscopy methods

Zhu, D., Cao, D., & Zhang, X. (2023) · Structure · doi:10.1016/j.str.2023.09.008 · Cited by 10

Human cells for human proteins: Isotope labeling in mammalian cells in suspension for functional NMR studies

Rößler, P., Ruckstuhl, M., Löbbert, A., Stühlinger, T. T., Franchini, L. R., Tsai, C., Lichtenecker, R. J., Shrestha, B., Rüdisser, S., Konrat, R., et al. (2026) · Protein Science · doi:10.1002/pro.70515 · Cited by 10

Kryo‐Elektronenmikroskopie als Methode für die strukturbasierte Wirkstoffentwicklung

Merino, F., & Raunser, S. (2016) · Angewandte Chemie · doi:10.1002/ange.201608432 · Cited by 10

Liquid electron microscopy: then, now and future

Bharda, A. V., & Jung, H. S. (2019) · Han-guk hyeonmigyeong hakoeji/Applied microscopy · doi:10.1186/s42649-019-0011-7 · Cited by 10

Cryo-electron microscopy of the giant viruses

Burton‐Smith, R. N., & Murata, K. (2021) · Microscopy · doi:10.1093/jmicro/dfab036 · Cited by 10

Emerging Quantitative Biochemical, Structural, and Biophysical Methods for Studying Ribosome and Protein–RNA Complex Assembly

Gor, K., & Duss, O. (2023) · Biomolecules · doi:10.3390/biom13050866 · Cited by 10

Miniaturized Sample Preparation for Transmission Electron Microscopy

Schmidli, C., Rima, L., Arnold, S. A., Stohler, T., Syntychaki, A., Bieri, A., Albiez, S., Goldie, K. N., Chami, M., Stahlberg, H., et al. (2018) · Journal of Visualized Experiments · doi:10.3791/57310 · Cited by 10

Recent progress in structural biology: lessons from our research history

Nitta, R., Imasaki, T., & Nitta, E. (2018) · Microscopy · doi:10.1093/jmicro/dfy022 · Cited by 10

Noncovalent Functionalization of Carbon Substrates with Hydrogels Improves Structural Analysis of Vitrified Proteins by Electron Cryo-Microscopy

Scherr, J., Neuhaus, A., Parey, K., Klusch, N., Murphy, B. J., Zickermann, V., Kühlbrandt, W., Terfort, A., & Rhinow, D. (2019) · ACS Nano · doi:10.1021/acsnano.9b02651 · Cited by 10

Protein Aggregation in a Nutshell: The Splendid Molecular Architecture of the Dreaded Amyloid Fibrils

Horváth, D., Menyhárd, D. K., & Perczel, A. (2019) · Current Protein and Peptide Science · doi:10.2174/1389203720666190925102832 · Cited by 9

Single-Particle Cryo-EM of Membrane Proteins in Lipid Nanodiscs

Kalienkova, V., Alvadia, C., Mosina, V. C., & Paulino, C. (2020) · Methods in molecular biology · doi:10.1007/978-1-0716-0373-4_17 · Cited by 10

Mycobacterium tuberculosis ferritin: a suitable workhorse protein for cryo-EM development

Gijsbers, A., Zhang, Y., Gao, Y., Peters, P. J., & Ravelli, R. B. G. (2021) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798321007233 · Cited by 10

Structure of filamentous viruses

Zanotti, G., & Grinzato, A. (2021) · Current Opinion in Virology · doi:10.1016/j.coviro.2021.09.006 · Cited by 10

Integrative illustration of a JCVI-syn3A minimal cell

Goodsell, D. S. (2022) · Berichte aus der medizinischen Informatik und Bioinformatik/Journal of integrative bioinformatics · doi:10.1515/jib-2022-0013 · Cited by 10

Cyanine Dye Coupling Mediates Self‐assembly of a pH Sensitive Peptide into Novel 3D Architectures

Fernandes, R. J., Chowdhary, S., Mikula, N., Saleh, N., Kanevche, K., von Berlepsch, H., Hosogi, N., Heberle, J., Weber, M., Böttcher, C., et al. (2022) · Angewandte Chemie International Edition · doi:10.1002/anie.202208647 · Cited by 10

Analytic modeling of inhomogeneous-resolution maps in cryo-electron microscopy and crystallography

Urzhumtsev, A., & Lunin, V. Y. (2022) · IUCrJ · doi:10.1107/s2052252522008260 · Cited by 16

Cryo-EM and Single-Particle Analysis with Scipion

Jiménez-Moreno, A., del Caño, L., Martínez, M., Ramírez-Aportela, E., Cuervo, A., Melero, R., Sánchez-García, R., Střelák, D., Fernández-Giménez, E., de Isidro-Gómez, F. P., et al. (2021) · Journal of Visualized Experiments · doi:10.3791/62261-v · Cited by 10

Cryo‐Correlative Light and Electron Microscopy

Bharat, T. A. M., & Kukulski, W. (2019) · doi:10.1002/9781119086420.ch8 · Cited by 10

Reaching the potential of electron diffraction

Acehan, D., Spoth, K. A., Budziszewski, G. R., Snell, M. E., Campomizzi, C. S., Lynch, M. L., & Bowman, S. E. J. (2024) · Cell Reports Physical Science · doi:10.1016/j.xcrp.2024.102007 · Cited by 9

Generating Multistate Conformations of P-type ATPases with a Conditional Diffusion Model

Xu, J., & Wang, Y. (2024) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.4c01519 · Cited by 9

Nonbonded Force Field Parameters Derived from Atoms-in-Molecules Methods Reproduce Interactions in Proteins from First-Principles

Castillo-Orellana, C., Heidar‐Zadeh, F., & Vöhringer‐Martinez, E. (2025) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.4c01406 · Cited by 9

Commonsense and common nonsense opinions: PROSPECTS for further reducing beam damage in electron microscopy of radiation-sensitive specimens

Glaeser, R. M. (2025) · Ultramicroscopy · doi:10.1016/j.ultramic.2025.114118 · Cited by 9

Radiation damage behavior of soft matter in ultrafast cryo-electron microscopy (cryo-UEM)

Zhao, Y., Chen, Q. H., Zhu, C., Zhu, Y., Zhang, Y., Gu, T., Tian, H., Wang, W., Huang, S., Yang, H., et al. (2025) · The Innovation Life · doi:10.59717/j.xinn-life.2025.100145 · Cited by 9

A comprehensive application of FiveFold for conformation ensemble-based protein structure prediction

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