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

From quantum to subcellular scales: multi-scale simulation approaches and the SIRAH force field

Machado, M. R., Zeida, A., Darré, L., & Pantano, S. (2019) · Interface Focus · doi:10.1098/rsfs.2018.0085 · Cited by 21

Synthesis and Characterization of Thiolate-Protected Gold Nanoparticles of Controlled Diameter

Shaltiel, L., Shemesh, A., Raviv, U., Barenholz, Y., & Levi‐Kalisman, Y. (2019) · The Journal of Physical Chemistry C · doi:10.1021/acs.jpcc.9b08817 · Cited by 21

Beyond protein structure determination with MicroED

Nguyen, C., & Gonen, T. (2020) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2020.05.018 · Cited by 21

From cells to atoms: Cryo‐EM as an essential tool to investigate pathogen biology, host–pathogen interaction, and drug discovery

Shepherd, D. C., Dalvi, S., & Ghosal, D. (2021) · Molecular Microbiology · doi:10.1111/mmi.14820 · Cited by 21

The EIGER detector for low-energy electron microscopy and photoemission electron microscopy

Tinti, G., Marchetto, H., Vaz, C. A. F., Kleibert, A., Andrä, M., Barten, R., Bergamaschi, A., Brückner, M., Cartier, S., Dinapoli, R., et al. (2017) · Journal of Synchrotron Radiation · doi:10.1107/s1600577517009109 · Cited by 21

Combining Mass Spectrometry (MS) and Nuclear Magnetic Resonance (NMR) Spectroscopy for Integrative Structural Biology of Protein–RNA ComplexesPreprint

Leitner, A., Dorn, G., & Allain, F. H. ‐. (2019) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a032359 · Cited by 21

Sequence-assignment validation in cryo-EM models with checkMySequence

Chojnowski, G. (2022) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798322005009 · Cited by 20

High-resolution protein modeling through Cryo-EM and AI: current trends and future perspectives – a review

Jeyaraj, G., Rajendran, A. K., Sathishkumar, K., Almutairi, B. O., Vadivelu, A., Chokkakula, S., Tu, Y., & Xie, W. (2025) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2025.1688455 · Cited by 25

A guide to quantifying membrane protein dynamics in lipids and other native‐like environments by solution‐state NMR spectroscopy

Bibow, S., & Hiller, S. (2018) · FEBS Journal · doi:10.1111/febs.14639 · Cited by 20

Machine Learning for Structure Determination in Single-Particle Cryo-Electron Microscopy: A Systematic Review

Wu, J., Yang, Y. X., Zhang, D., Liu, B., Zheng, Q., Xie, X., Liu, S.-Q., Ge, S., Hou, Z., & Xia, N. (2021) · IEEE Transactions on Neural Networks and Learning Systems · doi:10.1109/tnnls.2021.3131325 · Cited by 21

Exploring cryo-electron microscopy with molecular dynamics

Vant, J., Sarkar, D., Nguyen, J. T., Baker, A. T., Vermaas, J. V., & Singharoy, A. (2022) · Biochemical Society Transactions · doi:10.1042/bst20210485 · Cited by 20

Deciphering a hexameric protein complex with Angstrom optical resolution

Mazal, H., Wieser, F.-F., & Sandoghdar, V. (2022) · eLife · doi:10.7554/elife.76308 · Cited by 20

Conformation Dynamics of Single Polymer Strands in Solution

Bae, Y., Ha, M. Y., Bang, K., Yang, S., Kang, S. Y., Kim, J., Sung, J., Kang, S., Kang, D., Lee, W. B., et al. (2022) · Advanced Materials · doi:10.1002/adma.202202353 · Cited by 19

Developing Graphene Grids for Cryoelectron Microscopy

Fan, H., & Sun, F. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.937253 · Cited by 20

Protein model refinement for cryo-EM maps using AlphaFold 2 and the DAQ score

Terashi, G., Wang, X., & Kihara, D. (2022) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798322011676 · Cited by 23

Biophysical basis of filamentous phage tactoid-mediated antibiotic tolerance in P. aeruginosa

Böhning, J., Graham, M., Letham, S. C., Davis, L. K., Schulze, U., Stansfeld, P. J., Corey, R. A., Pearce, P., Tarafder, A. K., & Bharat, T. A. M. (2023) · Nature Communications · doi:10.1038/s41467-023-44160-8 · Cited by 20

Chloroplast ATP synthase: From structure to engineering

Rühle, T., Leister, D., & Pasch, V. (2024) · The Plant Cell · doi:10.1093/plcell/koae081 · Cited by 22

Solving the scalability issue in quantum-based refinement: Q|R#1

Zheng, M., Moriarty, N. W., Xu, Y., Reimers, J. R., Afonine, P. V., & Waller, M. P. (2017) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798317016746 · Cited by 20

Likelihood-based structural analysis of electron microscopy images

Cossio, P., & Hummer, G. (2018) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2018.03.004 · Cited by 20

Damage in electron cryomicroscopy: Lessons from biology for materials science

Russo, C., & Egerton, R. (2019) · MRS bulletin · doi:10.1557/mrs.2019.284 · Cited by 14

The current chemical biology tool box for studying ion channels

Braun, N., Sheikh, Z. P., & Pless, S. A. (2020) · The Journal of Physiology · doi:10.1113/jp276695 · Cited by 22

CryoPoseNet: End-to-End Simultaneous Learning of Single-particle Orientation and 3D Map Reconstruction from Cryo-electron Microscopy Data

Nashed, Y. S. G., Poitevin, F., Gupta, H., Woollard, G., Kagan, M., Yoon, C. H., & Ratner, D. F. (2021) · IEEE International Conference on Computer Vision Workshops · doi:10.1109/iccvw54120.2021.00452 · Cited by 20

Validation analysis of EMDB entries

Wang, Z., Patwardhan, A., & Kleywegt, G. J. (2022) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s205979832200328x · Cited by 20

Cryo2StructData: A Large Labeled Cryo-EM Density Map Dataset for AI-based Modeling of Protein Structures

Giri, N., Wang, L., & Cheng, J. (2024) · Scientific Data · doi:10.1038/s41597-024-03299-9 · Cited by 17

DiffInt: A Diffusion Model for Structure-Based Drug Design with Explicit Hydrogen Bond Interaction Guidance

Sako, M., Yasuo, N., & Sekijima, M. (2025) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.4c01385 · Cited by 21

Small LEA proteins mitigate air-water interface damage to fragile cryo-EM samples during plunge freezing

Abe, K. M., Gan, L., He, Q., Grant, T., & Lim, C. J. (2024) · Nature Communications · doi:10.1038/s41467-024-52091-1 · Cited by 20

Detecting Protein Communities in Native Cell Extracts by Machine Learning: A Structural Biologist’s Perspective

Kyrilis, F. L., Belapure, J., & Kastritis, P. L. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.660542 · Cited by 19

Direct visualization of floppy two-dimensional DNA origami using cryogenic electron microscopy

Ni, H., Fan, X., Zhou, F., Guo, G., Lee, J. Y., Seeman, N. C., Kim, D., Yao, N., Chaikin, P. M., & Han, Y. (2022) · iScience · doi:10.1016/j.isci.2022.104373 · Cited by 19

Cryo-EM of the injectisome and type III secretion systems

Bergeron, J. R. C., & Marlovits, T. C. (2022) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2022.102403 · Cited by 19

Developing novel antifungals: lessons from G protein-coupled receptors

Velazhahan, V., McCann, B. L., Bignell, E., & Tate, C. G. (2023) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2022.12.002 · Cited by 20

The Advances and Limitations of the Determination and Applications of Water Structure in Molecular Engineering

Zsidó, B. Z., Bayarsaikhan, B., Börzsei, R., Szél, V., Mohos, V., & Hetényi, C. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241411784 · Cited by 21

Scaling up cryo-EM for biology and chemistry: The journey from niche technology to mainstream method

de la Cruz, M. J., & Eng, E. T. (2023) · Structure · doi:10.1016/j.str.2023.09.009 · Cited by 19

A comparative study of single-particle cryo-EM with liquid-nitrogen and liquid-helium cooling

Pfeil-Gardiner, O., Mills, D. J., Vonck, J., & Kühlbrandt, W. (2019) · IUCrJ · doi:10.1107/s2052252519011503 · Cited by 19

Towards capture of dynamic assembly and action of the T3SS at near atomic resolution

Hu, J., Worrall, L. J., & Strynadka, N. C. J. (2019) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2019.10.005 · Cited by 19

In-Line Holography in Transmission Electron Microscopy for the Atomic Resolution Imaging of Single Particle of Radiation-Sensitive Matter

Carlino, E. (2020) · Materials · doi:10.3390/ma13061413 · Cited by 19

Gum-Net: Unsupervised Geometric Matching for Fast and Accurate 3D Subtomogram Image Alignment and Averaging

Zeng, X., & Xu, M. (2020) · IEEE Computer Society Conference on Computer Vision and Pattern Recognition/Proceedings - IEEE Computer Society Conference on Computer Vision and Pattern Recognition/Proceedings · doi:10.1109/cvpr42600.2020.00413 · Cited by 19

Structure of the Pseudomonas aeruginosa PAO1 Type IV pilus

Ochner, H., Böhning, J., Wang, Z., Tarafder, A. K., Caspy, I., & Bharat, T. A. M. (2024) · PLoS Pathogens · doi:10.1371/journal.ppat.1012773 · Cited by 18

Structural insights into actin filament turnover

Oosterheert, W., Sanders, M. B., Bieling, P., & Raunser, S. (2025) · Trends in Cell Biology · doi:10.1016/j.tcb.2024.12.009 · Cited by 18

The macromolecular crystallography beamlines of the Helmholtz-Zentrum Berlin at the BESSY II storage ring: history, current status and future directions

Müeller, U., Barthel, T., Benz, L. S., Bon, V., Crosskey, T., Dieguez, C. G., Förster, R., Gless, C., Hauß, T., Heinemann, U., et al. (2025) · Journal of Synchrotron Radiation · doi:10.1107/s1600577525001110 · Cited by 24

Cryo-EM of Mitochondrial Complex I and ATP Synthase

Kühlbrandt, W., Carreira, L. A. M., & Yıldız, Ö. (2025) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-060724-110838 · Cited by 19

Critical assessment of AI-based protein structure prediction: Fundamental challenges and future directions in drug discovery

Niazi, S. (2025) · Computational and Structural Biotechnology Reports · doi:10.1016/j.csbr.2025.100064 · Cited by 20

Cryo-Electron Tomography

Plitzko, J. M., & Baumeister, W. P. (2019) · Springer handbooks · doi:10.1007/978-3-030-00069-1_4 · Cited by 18

Residue-based pharmacophore approaches to study protein–protein interactions

Shrestha, R., Fajardo, J. E., & Fiser, A. (2021) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2020.12.016 · Cited by 18

Role of surfactants in electron cryo-microscopy film preparation

Michon, B., López-Sánchez, U., Degrouard, J., Nury, H., Leforestier, A., Rio, E., Salonen, A., & Zoonens, M. A. (2023) · Biophysical Journal · doi:10.1016/j.bpj.2023.04.016 · Cited by 18

Facing the phase problem

Hendrickson, W. A. (2023) · IUCrJ · doi:10.1107/s2052252523006449 · Cited by 20

Promotion of oxidative phosphorylation by complex I-anchored carbonic anhydrases?

Braun, H., & Klusch, N. (2023) · Trends in Plant Science · doi:10.1016/j.tplants.2023.07.007 · Cited by 18

Novel Artificial Intelligence-Based Approaches for Ab Initio Structure Determination and Atomic Model Building for Cryo-Electron Microscopy

DiIorio, M. C., & Kulczyk, A. (2023) · Micromachines · doi:10.3390/mi14091674 · Cited by 17

Direct Digital Electron Detectors

Clough, R., & Kirkland, A. I. (2016) · Advances in imaging and electron physics · doi:10.1016/bs.aiep.2016.09.001 · Cited by 18

Self-Perforated Hydrogel Nanomembranes Facilitate Structural Analysis of Proteins by Electron Cryo-Microscopy

Scherr, J., Parey, K., Klusch, N., Murphy, B. J., Balser, S., Neuhaus, A., Zickermann, V., Kühlbrandt, W., Terfort, A., & Rhinow, D. (2017) · ACS Nano · doi:10.1021/acsnano.7b03099 · Cited by 18

Structural analysis of pleomorphic and asymmetric viruses using cryo-electron tomography and subtomogram averaging

Obr, M., & Schur, F. K. M. (2019) · Advances in virus research · doi:10.1016/bs.aivir.2019.07.008 · Cited by 19

Assessing the JEOL CRYO ARM 300 for high-throughput automated single-particle cryo-EM in a multiuser environment

Fislage, M., Shkumatov, A. V., Stroobants, A., & Efremov, R. G. (2020) · IUCrJ · doi:10.1107/s2052252520006065 · Cited by 18

Structural insights into the architecture and assembly of eukaryotic flagella

Petriman, N.-A., & Lorentzen, E. (2020) · Microbial Cell · doi:10.15698/mic2020.11.734 · Cited by 19

A fiducial-assisted strategy compatible with resolving small MFS transporter structures in multiple conformations using cryo-EM

Xie, P., Li, Y., Lamon, G., Kuang, H., Wang, D., & Traaseth, N. J. (2025) · Nature Communications · doi:10.1038/s41467-024-54986-5 · Cited by 17

Reducing the effects of radiation damage in cryo-EM using liquid helium temperatures

Dickerson, J. L., Naydenova, K., Peet, M. J., Wilson, H., Nandy, B., McMullan, G., Morrison, R., & Russo, C. J. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2421538122 · Cited by 17

Structure-Based Drug Design for Tuberculosis: Challenges Still Ahead

Bruch, E., Petrella, S., & Bellinzoni, M. (2020) · Applied Sciences · doi:10.3390/app10124248 · Cited by 13

Structural biology in the time of COVID-19: perspectives on methods and milestones

Lynch, M. L., Snell, E. H., & Bowman, S. E. J. (2021) · IUCrJ · doi:10.1107/s2052252521003948 · Cited by 18

Combining X-rays, neutrons and electrons, and NMR, for precision and accuracy in structure–function studies

Helliwell, J. R. (2021) · Acta Crystallographica Section A Foundations and Advances · doi:10.1107/s205327332100317x · Cited by 16

Conquer by cryo-EM without physically dividing

Lander, G. C., & Glaeser, R. M. (2021) · Biochemical Society Transactions · doi:10.1042/bst20210360 · Cited by 17

New Horizons in Structural Biology of Membrane Proteins: Experimental Evaluation of the Role of Conformational Dynamics and Intrinsic Flexibility

Puthenveetil, R., Christenson, E. T., & Vinogradova, O. (2022) · Membranes · doi:10.3390/membranes12020227 · Cited by 18

Structure and Aggregation Mechanisms in Amyloids

Almeida, Z. L., & Brito, R. M. M. (2020) · Vide Leaf, Hyderabad eBooks · doi:10.37247/pamolscs.1.2020.9 · Cited by 17

Exploring the Structural Variability of Dynamic Biological Complexes by Single-Particle Cryo-Electron Microscopy

DiIorio, M. C., & Kulczyk, A. (2022) · Micromachines · doi:10.3390/mi14010118 · Cited by 17

Labelling strategies for correlative light electron microscopy

Tanner, H., Sherwin, O., & Verkade, P. (2023) · Microscopy Research and Technique · doi:10.1002/jemt.24304 · Cited by 17

Big data in contemporary electron microscopy: challenges and opportunities in data transfer, compute and management

Poger, D., Yen, L., & Braet, F. (2023) · Histochemistry and Cell Biology · doi:10.1007/s00418-023-02191-8 · Cited by 22

Expanding insights from in situ cryo-EM

Hutchings, J., & Villa, E. (2024) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2024.102885 · Cited by 17

Structural Biology in the Multi-Omics Era

McCafferty, C. L., Verbeke, E. J., Marcotte, E. M., & Taylor, D. W. (2020) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.9b01164 · Cited by 18

RCSB Protein Data Bank resources for structure-facilitated design of mRNA vaccines for existing and emerging viral pathogens

Goodsell, D. S., & Burley, S. K. (2021) · Structure · doi:10.1016/j.str.2021.10.008 · Cited by 17

Macromolecular crystallography using microcrystal electron diffraction

Clabbers, M. T. B., & Xu, H. (2021) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798320016368 · Cited by 17

Editorial overview: Cryo Electron Microscopy: Exciting advances in CryoEM Herald a new era in structural biology

Chiu, W., & Downing, K. H. (2017) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2017.07.006 · Cited by 17

Allostery

Montserrat‐Canals, M., Cordara, G., & Krengel, U. (2025) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583524000209 · Cited by 19

Integrative approaches in cryogenic electron microscopy: Recent advances in structural biology and future perspectives

Banerjee, A., Bhakta, S., & Sengupta, J. (2021) · iScience · doi:10.1016/j.isci.2021.102044 · Cited by 16

Atomic model validation using the CCP-EM software suite

Joseph, A. P., Olek, M., Malhotra, S., Zhang, P., Cowtan, K. D., Burnley, B. T., & Winn, M. (2022) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s205979832101278x · Cited by 16

Computational design of transmembrane proteins

Zhu, J., & Lu, P. (2022) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2022.102381 · Cited by 16

Cryo-electron microscopy in the fight against COVID-19—mechanism of virus entry

Bodakuntla, S., Kuhn, C. C., Biertümpfel, C., & Mizuno, N. (2023) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2023.1252529 · Cited by 17

Emerging Trends in Cryo-EM-based Structural Studies of Neuropathological Amyloids

Mishra, S. (2023) · Journal of Molecular Biology · doi:10.1016/j.jmb.2023.168361 · Cited by 16

Nanowire Field-Effect Transistor Sensors

Zhang, A., Zheng, G., & Lieber, C. M. (2016) · Nanoscience and technology · doi:10.1007/978-3-319-41981-7_10 · Cited by 16

Integrative modelling of cellular assemblies

Joseph, A. P., Polles, G., Alber, F., & Topf, M. (2017) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2017.07.001 · Cited by 15

Weakly Supervised 3D Semantic Segmentation Using Cross-Image Consensus and Inter-Voxel Affinity Relations

Zhu, X. L., Chen, J. W., Zeng, X., Liang, J., Li, C., Liu, S., Behpour, S., & Xu, M. (2021) · IEEE/CVF International Conference on Computer Vision (ICCV) · doi:10.1109/iccv48922.2021.00283 · Cited by 16

Cryo-electron tomography: The power of seeing the whole picture

Baumeister, W. P. (2022) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2022.08.078 · Cited by 16

Orthogonal matrix retrieval in cryo-electron microscopy

Bhamre, T., Zhang, T., & Singer, A. (2015) · IEEE International Symposium on Biomedical Imaging (ISBI) · doi:10.1109/isbi.2015.7164051 · Cited by 16

A Versatile High-Vacuum Cryo-transfer System for Cryo-microscopy and Analytics

Tacke, S., Krzyžánek, V., Nüsse, H., Wepf, R. A., Klingauf, J., & Reichelt, R. (2016) · Biophysical Journal · doi:10.1016/j.bpj.2016.01.024 · Cited by 16

Three-dimensional reconstruction for coherent diffraction patterns obtained by XFEL

Nakano, M., Miyashita, O., Jonić, S., Song, C., Nam, D., Joti, Y., & Tama, F. (2017) · Journal of Synchrotron Radiation · doi:10.1107/s1600577517007767 · Cited by 16

Carboxysomes: The next frontier in biotechnology and sustainable solutions

Correa, S. S., Schultz, J., Huntington, B., Naschberger, A., & Rosado, A. S. (2024) · Biotechnology Advances · doi:10.1016/j.biotechadv.2024.108511 · Cited by 15

User-friendly, High-throughput, and Fully Automated Data Acquisition Software for Single-particle Cryo-electron Microscopy

Kumar, A., Surekha, P., Gulati, S., & Dutta, S. (2021) · Journal of Visualized Experiments · doi:10.3791/62832 · Cited by 15

Structural Biology Illuminates Molecular Determinants of Broad Ebolavirus Neutralization by Human Antibodies for Pan-Ebolavirus Therapeutic Development

Murin, C. D., Gilchuk, P., Crowe, J. E., & Ward, A. B. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2021.808047 · Cited by 13

Focused ion beam-scanning electron microscopy provides novel insights of drug delivery phenomena

Faber, T., McConville, J. T., & Lamprecht, A. (2024) · Journal of Controlled Release · doi:10.1016/j.jconrel.2023.12.048 · Cited by 16

Validating Resolution Revolution

Neumann, P., Dickmanns, A., & Ficner, R. (2018) · Structure · doi:10.1016/j.str.2018.10.028 · Cited by 15

Structural nanotechnology: three-dimensional cryo-EM and its use in the development of nanoplatforms for in vitro catalysis

de Ruiter, M. V., Klem, R., Luque, D., Cornelissen, J. J. L. M., & Castón, J. R. (2019) · Nanoscale · doi:10.1039/c8nr09204d · Cited by 15

Single Particle CryoEM: Potential for Further Improvement

Henderson, R. A., & Russo, C. J. (2019) · Microscopy and Microanalysis · doi:10.1017/s1431927619000758 · Cited by 15

Exploiting phage strategies to modulate bacterial transcription

Wahl, M. C., & Sen, R. (2019) · Transcription · doi:10.1080/21541264.2019.1684137 · Cited by 15

Studying transcription initiation by RNA polymerase with diffusion‐based single‐molecule fluorescence

Alhadid, Y. K., Chung, S., Lerner, E., Taatjes, D. J., Borukhov, S. I., & Weiss, S. (2017) · Protein Science · doi:10.1002/pro.3160 · Cited by 15

Orienting the future of bio-macromolecular electron microscopy

Sun, F. (2018) · Chinese Physics B · doi:10.1088/1674-1056/27/6/063601 · Cited by 15

Directed evolution for high functional production and stability of a challenging G protein-coupled receptor

Waltenspühl, Y., Jeliazkov, J. R., Kummer, L., & Plückthun, A. (2021) · Scientific Reports · doi:10.1038/s41598-021-87793-9 · Cited by 13

Cryo-EM as a powerful tool for drug discovery: recent structural based studies of SARS-CoV-2

Kim, H., & Jung, H. S. (2021) · Han-guk hyeonmigyeong hakoeji/Applied microscopy · doi:10.1186/s42649-021-00062-x · Cited by 14

High-resolution ab initio reconstruction enables cryo-EM structure determination of small particlesPreprint

Kim, K., Li, H., & Clarke, O. B. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.09.08.674935 · Cited by 30

Autocorrelation analysis for cryo-EM with sparsity constraints: Improved sample complexity and projection-based algorithms

Bendory, T., Khoo, Y., Kileel, J., Mickelin, O., & Singer, A. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2216507120 · Cited by 14

Evolution of Sequence and Structure of SARS-CoV-2 Spike Protein: A Dynamic Perspective

Sinha, A., Sangeet, S., & Roy, S. (2023) · ACS Omega · doi:10.1021/acsomega.3c00944 · Cited by 14

Insights into protein structure using cryogenic light microscopy

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High-resolution single-particle imaging at 100–200 keV with the Gatan Alpine direct electron detector

Chan, L. M., Courteau, B. J., Maker, A., Wu, M., Basanta, B., Mehmood, H., Bulkley, D. P., Joyce, D., Lee, B., Mick, S. E., et al. (2024) · Journal of Structural Biology · doi:10.1016/j.jsb.2024.108108 · Cited by 14

Deciphering the Tubulin Code

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Cryo-EM enters a new era

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Resolution Revolution—Seeing the Molecules of Life With Electron Cryomicroscopy

Segev, N., & Henderson, R. A. (2023) · Frontiers for Young Minds · doi:10.3389/frym.2023.1063909 · Cited by 1

Record-breaking protein images have applications for drug discovery

Miller, J. L. (2016) · Physics Today · doi:10.1063/pt.3.3254 · Cited by 3

The resolution revolution recent advances in cryoEM

Crowther, R. A. (2016) · Cited by 2

The resolution revolution revisited

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