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

Efficient and stable reconstitution of the ABC transporter BmrA for solid-state NMR studies

Kunert, B., Gardiennet, C., Lacabanne, D., Calles-Garcia, D., Falson, P., Jault, J., Meier, B. H., Pénin, F., & Böckmann, A. (2014) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2014.00005 · Cited by 35

The potential of cryo-electron microscopy for structure-based drug design

Boland, A., Chang, L., & Barford, D. (2017) · Essays in Biochemistry · doi:10.1042/ebc20170032 · Cited by 32

Influence of Lipid Mimetics on Gating of Ryanodine Receptor

Willegems, K., & Efremov, R. G. (2018) · Structure · doi:10.1016/j.str.2018.06.010 · Cited by 29

Atom Probe Tomography for 3D Structural and Chemical Analysis of Individual Proteins

Sundell, G., Hulander, M., Pihl, A., & Andersson, M. (2019) · Small · doi:10.1002/smll.201900316 · Cited by 29

Introduction to crystallographic refinement of macromolecular atomic models

Urzhumtsev, A., & Lunin, V. Y. (2019) · Crystallography Reviews · doi:10.1080/0889311x.2019.1631817 · Cited by 29

Studies of structural determinants of substrate binding in the Creatine Transporter (CreaT, SLC6A8) using molecular models

Colas, C., Banci, G., Martini, R., & Ecker, G. F. (2020) · Scientific Reports · doi:10.1038/s41598-020-63189-z · Cited by 30

Two-colour single-molecule photoinduced electron transfer fluorescence imaging microscopy of chaperone dynamics

Schubert, J., Schulze, A., Prodromou, C., & Neuweiler, H. (2021) · Nature Communications · doi:10.1038/s41467-021-27286-5 · Cited by 29

Covariance estimation using conjugate gradient for 3D classification in CRYO-EM

Andén, J., Katsevich, E., & Singer, A. (2015) · IEEE International Symposium on Biomedical Imaging (ISBI) · doi:10.1109/isbi.2015.7163849 · Cited by 29

Multivariate Statistical Analysis of Large Datasets: Single Particle Electron Microscopy

van Heel, M., Portugal, R. V., & Schatz, M. X. (2016) · Open Journal of Statistics · doi:10.4236/ojs.2016.64059 · Cited by 29

Structural rearrangements of the RNA polymerase III machinery during tRNA transcription initiation

Ramsay, E. P., & Vannini, A. (2017) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2017.11.005 · Cited by 29

Cryo-EM Studies of Pre-mRNA Splicing: From Sample Preparation to Model Visualization

Wilkinson, M. E., Lin, P.-C., Plaschka, C., & Nagai, K. (2018) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-070317-033410 · Cited by 27

Never at rest: insights into the conformational dynamics of ion channels from cryo‐electron microscopy

Lau, C. H. Y., Hunter, M. J., Stewart, A. G., Perozo, E., & Vandenberg, J. I. (2018) · The Journal of Physiology · doi:10.1113/jp274888 · Cited by 29

Visualization of biological macromolecules at near-atomic resolution: cryo-electron microscopy comes of age

MITRA, A. K. (2018) · Acta Crystallographica Section F Structural Biology Communications · doi:10.1107/s2053230x18015133 · Cited by 29

Characterizing the resolution and throughput of the Apollo direct electron detector

Peng, R., Fu, X., Mendez, J. H., Randolph, P. S., Bammes, B. E., & Stagg, S. M. (2022) · Journal of Structural Biology X · doi:10.1016/j.yjsbx.2022.100080 · Cited by 28

Determination of the Structure and Dynamics of the Fuzzy Coat of an Amyloid Fibril of IAPP Using Cryo-Electron Microscopy

Brotzakis, Z. F., Löhr, T., Truong, S. D., Hoff, S., Bonomi, M., & Vendruscolo, M. (2023) · Biochemistry · doi:10.1021/acs.biochem.3c00010 · Cited by 28

Touch, act and go: landing and operating on nucleosomes

Speranzini, V., Pilotto, S., Sixma, T. K., & Mattevi, A. (2016) · The EMBO Journal · doi:10.15252/embj.201593377 · Cited by 32

Quantitative assessment of chlorophyll types in cryo-EM maps of photosystem I acclimated to far-red light

Gisriel, C. J., Huang, H.-L., Reiss, K. M., Flesher, D. A., Batista, V. S., Bryant, D. A., Brudvig, G. W., & Wang, J. (2021) · BBA Advances · doi:10.1016/j.bbadva.2021.100019 · Cited by 28

Interaction of human erythrocyte catalase with air–water interface in cryoEM

Chen, S., Li, J., Vinothkumar, K. R., & Henderson, R. A. (2021) · Microscopy · doi:10.1093/jmicro/dfab037 · Cited by 28

CryoAI: Amortized Inference of Poses for Ab Initio Reconstruction of 3D Molecular Volumes from Real Cryo-EM Images

Levy, A., Poitevin, F., Martel, J., Nashed, Y. S. G., Peck, A., Miolane, N., Ratner, D. F., Dunne, M., & Wetzstein, G. (2022) · Lecture notes in computer science · doi:10.1007/978-3-031-19803-8_32 · Cited by 28

Quantitative Cryo-Electron Tomography

Navarro, P. P. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.934465 · Cited by 28

A Tale of Chromatin and Transcription in 100 Structures

Cramer, P. (2014) · Cell · doi:10.1016/j.cell.2014.10.047 · Cited by 28

Electron cryo-tomography captures macromolecular complexes in native environments

Baker, L. A., Grange, M., & Grünewald, K. (2017) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2017.08.005 · Cited by 29

Integrative/Hybrid Modeling Approaches for Studying Biomolecules

Srivastava, A., Tiwari, S. P., Miyashita, O., & Tama, F. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2020.01.039 · Cited by 29

Biostructural Science Inspired by Next-Generation X-Ray Sources

Gruner, S. M., & Lattman, E. E. (2015) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-060414-033813 · Cited by 27

Soft matter and nanomaterials characterization by cryogenic transmission electron microscopy

Watt, J. D., Huber, D. L., & Stewart, P. L. (2019) · MRS Bulletin · doi:10.1557/mrs.2019.285 · Cited by 27

Cryo-Electron microscopy for the study of self-assembled poly(ionic liquid) nanoparticles and protein supramolecular structures

Kochovski, Z., Chen, G., Yuan, J., & Lu, Y. Q. (2020) · Colloid & Polymer Science · doi:10.1007/s00396-020-04657-w · Cited by 27

IP3 receptors: An “elementary” journey from structure to signals

Smith, H. A., Thillaiappan, N. B., & Rossi, A. M. (2023) · Cell Calcium · doi:10.1016/j.ceca.2023.102761 · Cited by 26

An outlook on using serial femtosecond crystallography in drug discovery

Mishin, A., Gusach, A., Luginina, A. P., Marin, E., Borshchevskiy, V. I., & Cherezov, V. (2019) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2019.1626822 · Cited by 27

Heterogeneous Multireference Alignment for Images With Application to 2D Classification in Single Particle Reconstruction

Ma, C., Bendory, T., Boumal, N., Sigworth, F. J., & Singer, A. (2019) · IEEE Transactions on Image Processing · doi:10.1109/tip.2019.2945686 · Cited by 27

Using cryo-EM to understand antimycobacterial resistance in the catalase-peroxidase (KatG) from Mycobacterium tuberculosis

Munir, A., Wilson, M. T., Hardwick, S. W., Chirgadze, D. Y., Worrall, J. A. R., Blundell, T. L., & Chaplin, A. K. (2021) · Structure · doi:10.1016/j.str.2020.12.008 · Cited by 27

PyTME (Python Template Matching Engine): A fast, flexible, and multi-purpose template matching library for cryogenic electron microscopy data

Maurer, V. J., Siggel, M., & Kosiński, J. (2024) · SoftwareX · doi:10.1016/j.softx.2024.101636 · Cited by 26

Structural bioinformatics for rational drug design

Mozaffari, S., Moen, A., Ng, C. Y., Nicolaes, G. A. F., & Wichapong, K. (2025) · Research and Practice in Thrombosis and Haemostasis · doi:10.1016/j.rpth.2025.102691 · Cited by 31

Devitrification reduces beam-induced movement in cryo-EM

Wieferig, J.-P., Mills, D. J., & Kühlbrandt, W. (2021) · IUCrJ · doi:10.1107/s2052252520016243 · Cited by 26

Perspective towards atomic‐resolution imaging of two‐dimensional polymers

Qi, H., Liang, B., & Kaiser, U. A. (2021) · SmartMat · doi:10.1002/smm2.1035 · Cited by 26

The impact of AlphaFold2 on experimental structure solution

Edich, M., Briggs, D. C., Kippes, O., Gao, Y., & Thorn, A. (2022) · Faraday Discussions · doi:10.1039/d2fd00072e · Cited by 29

In-cell NMR: recent progresses and future challenges

Luchinat, E., & Banci, L. (2023) · RENDICONTI LINCEI · doi:10.1007/s12210-023-01168-y · Cited by 26

Separating distinct structures of multiple macromolecular assemblies from cryo-EM projections

Verbeke, E. J., Zhou, Y., Horton, A. P., Mallam, A. L., Taylor, D. W., & Marcotte, E. M. (2019) · Journal of Structural Biology · doi:10.1016/j.jsb.2019.107416 · Cited by 26

Cryo‐EM of ABC transporters: an ice‐cold solution to everything?

Januliene, D., & Moeller, A. (2020) · FEBS Letters · doi:10.1002/1873-3468.13989 · Cited by 26

CryoSeek: A strategy for bioentity discovery using cryoelectron microscopy

Wang, T., Li, Z., Xu, K., Huang, W., Huang, G., Zhang, Q. C., & Yan, N. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2417046121 · Cited by 26

Ultracold cryogenic TEM with liquid helium and high stability

Rennich, E., Sung, S., Agarwal, N., Gates, M., Kerns, R., Hovden, R., & Baggari, I. E. (2024) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.2509736122 · Cited by 19

Description and comparison of algorithms for correcting anisotropic magnification in cryo-EM images

Zhao, J., Brubaker, M. A., Benlekbir, S., & Rubinstein, J. L. (2015) · Journal of Structural Biology · doi:10.1016/j.jsb.2015.06.014 · Cited by 25

Multi-target detection with application to cryo-electron microscopy

Bendory, T., Boumal, N., Leeb, W., Levin, E., & Singer, A. (2019) · Inverse Problems · doi:10.1088/1361-6420/ab2aec · Cited by 25

Types and Functions of Mitoribosome-Specific Ribosomal Proteins across Eukaryotes

Scaltsoyiannes, V., Corre, N., Waltz, F., & Giegé, P. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23073474 · Cited by 26

Native-like environments afford novel mechanistic insights into membrane proteins

Notti, R. Q., & Walz, T. (2022) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2022.02.008 · Cited by 25

Quantitative mining of compositional heterogeneity in cryo-EM datasets of ribosome assembly intermediates

Rabuck-Gibbons, J. N., Lyumkis, D., & Williamson, J. R. (2022) · Structure · doi:10.1016/j.str.2021.12.005 · Cited by 25

Biophysical Screening Pipeline for Cryo-EM Grid Preparation of Membrane Proteins

Niebling, S., Veith, K., Vollmer, B., Lizarrondo, J., Burastero, O., Schiller, J., García, A. S., Lewe, P., Seuring, C., Witt, S., et al. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.882288 · Cited by 26

3D reconstruction of two-dimensional crystals

Stahlberg, H., Biyani, N., & Engel, A. H. (2015) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2015.06.006 · Cited by 25

Using Cryo-EM to Investigate Bacterial Secretion Systems

Rapisarda, C., Tassinari, M., Gubellini, F., & Fronzes, R. (2018) · Annual Review of Microbiology · doi:10.1146/annurev-micro-090817-062702 · Cited by 25

Retrieving high-resolution information from disordered 2D crystals by single-particle cryo-EM

Righetto, R. D., Biyani, N., Kowal, J., Chami, M., & Stahlberg, H. (2019) · Nature Communications · doi:10.1038/s41467-019-09661-5 · Cited by 25

The resolution revolution in X-ray diffraction, Cryo-EM and other Technologies

Blundell, T. L., & Chaplin, A. K. (2021) · Progress in Biophysics and Molecular Biology · doi:10.1016/j.pbiomolbio.2021.01.003 · Cited by 25

Validating Resolution Revolution

Neumann, P., Dickmanns, A., & Ficner, R. (2018) · Structure · doi:10.1016/j.str.2018.03.004 · Cited by 25

CryoAtom improves model building for cryo-EM

Su, B., Huang, K., Peng, Z., Amunts, A., & Yang, J. (2025) · Nature Structural & Molecular Biology · doi:10.1038/s41594-025-01713-3 · Cited by 39

Liquid-Phase Transmission Electron Microscopy for Reliable In Situ Imaging of Nanomaterials

Sung, J., Bae, Y., Park, H., Kang, S., Choi, B. K., Kim, J., & Park, J. (2022) · Annual Review of Chemical and Biomolecular Engineering · doi:10.1146/annurev-chembioeng-092120-034534 · Cited by 24

Experimental phasing opportunities for macromolecular crystallography at very long wavelengths

Omari, K. E., Duman, R., Mykhaylyk, V. B., Orr, C. M., Latimer-Smith, M., Winter, G., Grama, V., Qu, F., Bountra, K., Kwong, H.-S., et al. (2023) · Communications Chemistry · doi:10.1038/s42004-023-01014-0 · Cited by 26

Single-particle based helical reconstruction—how to make the most of real and Fourier space

Sachse, C. (2015) · AIMS Biophysics · doi:10.3934/biophy.2015.2.219 · Cited by 24

Validation of 3D EM Reconstructions: The Phantom in the Noise

Heymann, J. B. (2015) · AIMS Biophysics · doi:10.3934/biophy.2015.1.21 · Cited by 24

Visualizing Biological Membrane Organization and Dynamics

Baaden, M. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.02.018 · Cited by 24

Quo Vadis Biomolecular NMR Spectroscopy?

Selenko, P. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20061278 · Cited by 24

Development of “Plug and Play” Fiducial Marks for Structural Studies of GPCR Signaling Complexes by Single-Particle Cryo-EM

Dutka, P., Mukherjee, S., Gao, X., Kang, Y., de Waal, P. W., Wang, L., Zhuang, Y., Melcher, K., Zhang, C., Xu, H. E., et al. (2019) · Structure · doi:10.1016/j.str.2019.10.004 · Cited by 23

Permutation testing of Fourier shell correlation for resolution estimation of cryo-EM maps

Beckers, M., & Sachse, C. (2020) · Journal of Structural Biology · doi:10.1016/j.jsb.2020.107579 · Cited by 24

Electrospray-assisted cryo-EM sample preparation to mitigate interfacial effects

Yang, Z., Fan, J., Wang, J., Fan, X., Ouyang, Z., Wang, H., & Zhou, X. (2024) · Nature Methods · doi:10.1038/s41592-024-02247-0 · Cited by 23

Capturing a methanogenic carbon monoxide dehydrogenase/acetyl-CoA synthase complex via cryogenic electron microscopy

Biester, A., Grahame, D. A., & Drennan, C. L. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2410995121 · Cited by 24

Structural diversity and clustering of bacterial flagellar outer domains

Fields, J. L., Zhang, H., Bellis, N. F., Petersen, H. A., Halder, S. K., Rich-New, S. T., Krupovic, M., Wu, H., & Wang, F. (2024) · Nature Communications · doi:10.1038/s41467-024-53923-w · Cited by 23

Local resolution estimates of cryoEM reconstructions

Vilas, J. L., Heymann, J. B., Tagare, H., Ramírez-Aportela, E., Carazo, J. M., & Sorzano, C. Ó. S. (2020) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2020.06.005 · Cited by 23

Setting up and operating a cryo-EM laboratory

Mills, D. J. (2021) · Quarterly Reviews of Biophysics · doi:10.1017/s003358352000013x · Cited by 23

Moving toward generalizable NZ-1 labeling for 3D structure determination with optimized epitope-tag insertion

Tamura, R., Aruga, R., Hirose, M., Ekimoto, T., Miyake, T., Hizukuri, Y., Oi, R., Kaneko, M. K., Kato, Y., Akiyama, Y., et al. (2021) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798321002527 · Cited by 23

The rapid developments of membrane protein structure biology over the last two decades

Guan, L. (2023) · BMC Biology · doi:10.1186/s12915-023-01795-9 · Cited by 23

Two distinct archaeal type IV pili structures formed by proteins with identical sequence

Liu, J., Eastep, G. N., Cvirkaitė‐Krupovič, V., Rich-New, S. T., Kreutzberger, M. A. B., Egelman, E. H., Krupovìč, M., & Wang, F. (2024) · Nature Communications · doi:10.1038/s41467-024-45062-z · Cited by 23

Total Sample Conditioning and Preparation of Nanoliter Volumes for Electron Microscopy

Arnold, S. A., Albiez, S., Opara, N., Chami, M., Schmidli, C., Bieri, A., Padeste, C., Stahlberg, H., & Braun, T. (2016) · ACS Nano · doi:10.1021/acsnano.6b01328 · Cited by 23

Electron microscopy snapshots of single particles from single cells

Yi, X., Verbeke, E. J., Chang, Y., Dickinson, D. J., & Taylor, D. W. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.006686 · Cited by 23

Shining light on cysteine modification: connecting protein conformational dynamics to catalysis and regulation

van den Bedem, H., & Wilson, M. A. (2019) · Journal of Synchrotron Radiation · doi:10.1107/s160057751900568x · Cited by 25

Integration of Cryo-EM Model Building Software in Scipion

Martínez, M., Jiménez-Moreno, A., Maluenda, D., Ramírez-Aportela, E., Melero, R., Cuervo, A., Conesa, P., del Caño, L., Fonseca, Y. C., Sánchez-García, R., et al. (2020) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.9b01032 · Cited by 23

Automated cryo-EM sample preparation by pin-printing and jet vitrificationPreprint

Ravelli, R. B. G., Nijpels, F. J. T., Henderikx, R., Weissenberger, G., Thewessem, S., Gijsbers, A., Beulen, B. W. A. M. M., López‐Iglesias, C., & Peters, P. J. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/651208 · Cited by 23

An aldehyde-crosslinking mitochondrial probe for STED imaging in fixed cells

Chen, J., Stephan, T., Gaedke, F., Liu, T., Li, Y., Schauss, A. C., Chen, P., Wulff, V., Jakobs, S., Jüngst, C., et al. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2317703121 · Cited by 22

Actin filament dynamics at barbed ends: New structures, new insights

Courtemanche, N., & Henty-Ridilla, J. L. (2024) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2024.102419 · Cited by 22

Membrane Protein Complex ExbB 4 -ExbD 1 -TonB 1 from Escherichia coli Demonstrates Conformational Plasticity

Sverzhinsky, A., Chung, J. W., Deme, J. C., Fabre, L., Levey, K. T., Plesa, M., Carter, D. M., Lypaczewski, P., & Coulton, J. W. (2015) · Journal of Bacteriology · doi:10.1128/jb.00069-15 · Cited by 22

Integrative Modeling of Macromolecular Assemblies from Low to Near-Atomic Resolution

Xu, X., Yan, C., Wohlhueter, R. M., & Ivanov, I. N. (2015) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2015.08.005 · Cited by 23

Cryo-EM studies of the structure and dynamics of vacuolar-type ATPases

Mazhab‐Jafari, M. T., & Rubinstein, J. L. (2016) · Science Advances · doi:10.1126/sciadv.1600725 · Cited by 21

Purification of the key enzyme complexes of the anammox pathway from DEMON sludge

Akram, M., Dietl, A., Müller, M., & Barends, T. R. M. (2021) · Biopolymers · doi:10.1002/bip.23428 · Cited by 22

Frozen motion: how cryo-EM changes the way we look at ABC transporters

Shvarev, D., Januliene, D., & Moeller, A. (2021) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2021.11.008 · Cited by 22

Structures of synthetic helical filaments and tubes based on peptide and peptido-mimetic polymers

Miller, J. G., Hughes, S. A., Modlin, C., & Conticello, V. P. (2022) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583522000014 · Cited by 24

New insights into the mechanochemical coupling mechanism of kinesin–microtubule complexes from their high-resolution structures

Benoit, M. P. M. H., Hunter, B., Allingham, J. S., & Sosa, H. (2023) · Biochemical Society Transactions · doi:10.1042/bst20221238 · Cited by 20

Integrating AlphaFold and deep learning for atomistic interpretation of cryo-EM maps

Dai, X., Wu, L., Yoo, S., & Liu, Q. (2023) · Briefings in Bioinformatics · doi:10.1093/bib/bbad405 · Cited by 22

Structures of the Carbon-Phosphorus Lyase Complex Reveal the Binding Mode of the NBD-like PhnK

Yang, K., Ren, Z., Raushel, F. M., & Zhang, J. (2015) · Structure · doi:10.1016/j.str.2015.11.009 · Cited by 22

From the resolution revolution to evolution: structural insights into the evolutionary relationships between vesicle coats and the nuclear pore

Beck, M., Mosalaganti, S., & Kosiński, J. (2018) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2018.07.012 · Cited by 22

Three‐dimensional electron microscopy techniques for unravelling mitochondrial dysfunction in heart failure and identification of new pharmacological targets

Daghistani, H., Rajab, B. S., & Kitmitto, A. (2018) · British Journal of Pharmacology · doi:10.1111/bph.14499 · Cited by 22

Microsecond melting and revitrification of cryo samples with a correlative light-electron microscopy approach

(2022) · doi:10.3389/fmolb.2022.1044509 · Cited by 20

Array tomography: characterizing FAC‐sorted populations of zebrafish immune cells by their 3D ultrastructure

Wacker, I. U., Chockley, P. J., Bartels, C., Spomer, W., HOFMANN, A., Gengenbach, U. K., SINGH, S., Thaler, M., Grabher, C., & Schröder, R. R. (2015) · Journal of Microscopy · doi:10.1111/jmi.12223 · Cited by 21

CryoEM structures of spliceosomal complexes reveal the molecular mechanism of pre-mRNA splicing

Scheres, S. H. W., & Nagai, K. (2017) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2017.08.001 · Cited by 21

Structure–Function Relationship and Physiological Roles of Transient Receptor Potential Canonical (TRPC) 4 and 5 Channels

Kim, J., Ko, J., Hong, C., & So, I. (2019) · Cells · doi:10.3390/cells9010073 · Cited by 21

2.7 Å cryo-EM structure of vitrified M. musculus H-chain apoferritin from a compact 200 keV cryo-microscope

Hamdi, F., Tüting, C., Semchonok, D. A., Visscher, K. M., Kyrilis, F. L., Meister, A., Skalidis, I., Schmidt, L., Parthier, C., Stubbs, M. T., et al. (2020) · PLoS ONE · doi:10.1371/journal.pone.0232540 · Cited by 21

Structural interpretation of cryo-EM image reconstructions

Beckers, M., Mann, D., & Sachse, C. (2020) · Progress in Biophysics and Molecular Biology · doi:10.1016/j.pbiomolbio.2020.07.004 · Cited by 21

Superimposition of Viral Protein Structures: A Means to Decipher the Phylogenies of Viruses

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Microcrystal electron diffraction in macromolecular and pharmaceutical structure determination

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Understanding the Electron Beam Resilience of Two-Dimensional Conjugated Metal–Organic Frameworks

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A snapshot love story: what serial crystallography has done and will do for us

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Robust evaluation of 3D electron cryomicroscopy data using tilt-pairs

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Biological Applications at the Cutting Edge of Cryo-Electron Microscopy

Dillard, R. S., Hampton, C. M., Strauss, J. D., Ke, Z., Altomara, D., Guerrero-Ferreira, R., Kiss, G., & Wright, E. R. (2018) · Microscopy and Microanalysis · doi:10.1017/s1431927618012382 · Cited by 21

Capabilities of the Falcon III detector for single-particle structure determination

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Cryo-EM enters a new era

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Resolution Revolution—Seeing the Molecules of Life With Electron Cryomicroscopy

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Record-breaking protein images have applications for drug discovery

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The resolution revolution recent advances in cryoEM

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The resolution revolution revisited

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