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

Evaluating direct detection detectors for short-range order characterization of amorphous materials by electron scattering

Basha, A., Lévi, G., Houben, L., Amrani, T., Goldfarb, I., & Kohn, A. (2023) · Ultramicroscopy · doi:10.1016/j.ultramic.2023.113737 · Cited by 3

Enhancing spatial resolution in MÖNCH for electron microscopy via deep learning

Xie, X., Flores, L. B., Béjar, B., Bergamaschi, A., Fröjdh, E., Müller, E. A., Paton, K. A., Poghosyan, E., & Remlinger, C. (2024) · Journal of Instrumentation · doi:10.1088/1748-0221/19/01/c01020 · Cited by 3

Mass Spectrometry Investigation of Some ATP-Binding Cassette (ABC) Proteins

Agostini, M., Traldi, P., & Hamdan, M. H. (2024) · Medicina · doi:10.3390/medicina60020200 · Cited by 3

Good reasons for structural biology

Cramer, P. (2024) · Nature Structural & Molecular Biology · doi:10.1038/s41594-024-01232-7 · Cited by 3

The underlying mechanisms of arenaviral entry through matriglycan

Katz, M., & Diskin, R. (2024) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2024.1371551 · Cited by 4

Insights into conformational changes in cytochrome b during the early steps of its maturation

Carlström, A., & Ott, M. (2024) · FEBS Letters · doi:10.1002/1873-3468.14888 · Cited by 3

A Data Set of Paired Structural Segments Between Protein Data Bank and AlphaFold DB for Medium-Resolution Cryo-EM Density Maps: A Gap in Overall Structural Quality

Nguyen, T. H., Wriggers, W. R., & He, J. J. (2024) · Lecture notes in computer science · doi:10.1007/978-981-97-5087-0_5 · Cited by 3

Parallelizing cryo-EM 3D reconstruction on GPU cluster with a partitioned and streamed model

Wang, K., Xu, S., Fu, H., Yu, H., Zhao, W., & Yang, G. (2019) · International Conference on Supercomputing · doi:10.1145/3330345.3330347 · Cited by 3

Initial Results from the CryoARM300 and DE-64 Counting

Bammes, B. E., Spilman, M. S., Streetley, J., & Bhella, D. (2019) · Microscopy and Microanalysis · doi:10.1017/s1431927619005737 · Cited by 3

A Histogram-based Outlier Profile for Atomic Structures Derived from Cryo-Electron Microscopy

Chen, L., & He, J. J. (2019) · ACM International Conference on Bioinformatics, Computational Biology, and Health Informatics (ACM-BCB) · doi:10.1145/3307339.3343865 · Cited by 3

Forecasting Model for the Annual Growth of Cryogenic Electron Microscopy Data

Al-Haija, Q. S. A., & Nasr, K. A. (2020) · Lecture notes in computer science · doi:10.1007/978-3-030-46165-2_12 · Cited by 3

Macromolecular X-ray crystallography: soon to be a road less travelled?

Beale, J. H. (2020) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798320004660 · Cited by 3

Single Particle Cryo-Electron Microscopy: From Sample to Structure

White, J. B. R., Maskell, D. P., Howe, A., Harrow, M., Clare, D. K., Siebert, C. A., Hesketh, E. L., & Thompson, R. F. (2021) · Journal of Visualized Experiments · doi:10.3791/62415-v · Cited by 3

Real-time and decision taking selection of single-particles during automated cryo-EM sessions based on neuro-fuzzy method

Gil‐Carton, D., Zamora, M., Sutherland, J. D., Barrio, R., Garrido, I., Valle, M., & Garrido, A. J. (2016) · Expert Systems with Applications · doi:10.1016/j.eswa.2016.02.018 · Cited by 3

Analysis of nano-crystals: Evaluation of heavy metal-embedded biological specimen by high voltage electron microscopy

Jeong, H., Yoo, S. J., Won, J., Lee, H., Chung, J. M., Kim, H., Kim, G. J., Kim, J.-G., Jung, H. S., & Hyun, J. (2018) · Ultramicroscopy · doi:10.1016/j.ultramic.2018.07.003 · Cited by 3

Preparation of filamentous proteins for electron microscopy visualization and reconstruction

Matyszewski, M., & Sohn, J. (2019) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2019.06.007 · Cited by 3

Tailored Suits Fit Better: Customized Protein Crystallization Screens

Mlynek, G., Košťan, J., Leeb, S., & Djinović‐Carugo, K. (2019) · Crystal Growth & Design · doi:10.1021/acs.cgd.9b01328 · Cited by 3

EMPAS: Electron Microscopy Screening for Endogenous Protein Architectures.

Kim, G., Jang, S., Lee, E., & Song, J. (2020) · PubMed Central · doi:10.14348/molcells.2020.0163 · Cited by 3

Advanced Technologies for Protein Complex Production and Characterization

Vega, M. C., & Fernández, F. J. (2024) · Advances in experimental medicine and biology · doi:10.1007/978-3-031-52193-5 · Cited by 2

Concluding remarks: Challenges and future developments in biological electron cryo-microscopy

Kühlbrandt, W. (2022) · Faraday Discussions · doi:10.1039/d2fd90062a · Cited by 3

Generative Adversarial Networks for Robust Cryo-EM Image Denoising

Gu, H., Xian, Y., Unarta, I. C., & Yao, Y. (2023) · Springer eBooks · doi:10.1007/978-3-030-98661-2_126 · Cited by 3

Membrane Protein Crystallization

Tsai, C., & Schertler, G. F. X. (2020) · doi:10.1002/9781118681121.ch9 · Cited by 3

Computational Methods for Single-Particle Cryo-EMPreprint

Singer, A., & Sigworth, F. J. (2020) · arXiv (Cornell University) · doi:10.48550/arxiv.2003.13828 · Cited by 3

Robust Autoencoder GAN for Cryo-EM Image DenoisingPreprint

Gu, H., Unarta, I. C., Huang, X., & Yao, Y. (2020) · arXiv (Cornell University) · Cited by 3

Analytic representation of inhomogeneous-resolution maps of three-dimensional scalar fieldsPreprint

Urzhumtsev, A., & Lunin, V. Y. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.03.28.486044 · Cited by 3

Preface

Crowther, R. A. (2016) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(16)30228-2 · Cited by 3

Optimized path planning surpasses human efficiency in cryo-EM imagingPreprint

Li, Y., Fan, Q., Xu, Z., Lee, E. R., Cohn, J., Demers, V., Lee, J. Y., Yip, L., Cianfrocco, M. A., & Vos, S. M. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.06.17.496614 · Cited by 2

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 F Structural Biology Communications · doi:10.1107/s2053230x23004934 · Cited by 3

Mechanisms of transcription and RNA processing

Passmore, L. A., & Zhang, S. (2024) · Nature Structural & Molecular Biology · doi:10.1038/s41594-024-01312-8 · Cited by 3

High-resolution mastigoneme structure reveals 5’,5’-phosphodiesters stabilized glycan foldingPreprint

Huang, J., Tao, H., Chen, J., Pan, J., Yan, C., & Yan, N. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.12.24.630281 · Cited by 3

The 8-nm spaghetti: well-structured glycans coating linear tetrapeptide repeats discovered from freshwater with CryoSeekPreprint

Wang, T., Sun, Y., Li, Z., & Yan, N. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.12.15.627649 · Cited by 3

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 · doi:10.1002/ange.202208647 · Cited by 2

Ligand-Conditioned Side Chain Packing for Flexible Molecular Docking

Luo, D., Qu, X., Lu, D., Wang, Y., Dong, L., & Wang, B. (2025) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.4c01636 · Cited by 3

Structural Biology: Current Trends and Future Perspectives

Mishra, A., Khan, K., & Kumar, D. (2025) · Springer eBooks · doi:10.1007/978-981-96-2088-3_11 · Cited by 2

Unraveling atomic complexity from frozen samples

Ruma, Y. N., Nannenga, B. L., & Gonen, T. (2025) · Structural Dynamics · doi:10.1063/4.0000303 · Cited by 2

Improved cryo-EM reconstruction of sub-50 kDa complexes using 2D template matching

Zhang, K., Grant, T., & Grigorieff, N. (2026) · eLife · doi:10.1101/2025.09.11.675606 · Cited by 2

Cryo-EM Structure of the Cyclase Domain and Evaluation of Substrate Channeling in a Bifunctional Class II Terpene Synthase

Gaynes, M. N., Schultz, K. C., Wenger, E. S., Ronnebaum, T. A., Marmorstein, R., & Christianson, D. W. (2025) · Biochemistry · doi:10.1021/acs.biochem.5c00509 · Cited by 2

Impurities in amyloid studies: The power of automated model building within a cautionary tale for structural biologists

Rhyner, D., Frey, L., Zhou, J., Kwiatkowski, W., Mezzenga, R., Riek, R., & Greenwald, J. (2025) · Protein Science · doi:10.1002/pro.70353 · Cited by 2

A bundled anti-parallel cytochrome nanowire structure suggests roles in cell-cell electron transfer and biofilm formation

Petersen, H. A., Chan, C. H., Carpenter, G. O., Tabari, M. Z., Fields, J. L., Zia, A., Rich-New, S. T., Hochbaum, A. I., Bond, D. R., & Wang, F. (2026) · mBio · doi:10.1128/mbio.00906-26 · Cited by 1

In situ structural analysis of mammalian cells using a 200 kV electron cryomicroscope – implications for research infrastructure

Szwedziak, P. (2025) · BMC Methods · doi:10.1186/s44330-025-00047-2 · Cited by 4

Nucleotide Exchange Mechanism Involving Angle-Dependent Rate Constants Extracted from F1-ATPase Single-Molecule Rotation Trajectories

Volkán-Kacsó, S., Matute, R. A., Michel‐Beyerle, M. E., Khatchikian, O., & Marcus, R. A. (2025) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.5c04403 · Cited by 2

Structures of CRP antigen-antibody complexes provide insights into the mechanism of specific recognition

Li, Y., Yu, Q., Du, M., Zhang, J., Liu, T., Wang, J., Wei, Q., Peng, Y., Duan, C., Gu, D., et al. (2025) · Communications Biology · doi:10.1038/s42003-025-08941-9 · Cited by 2

Recent Methods from Statistical Inference for Integrative Structural Modeling

Arvindekar, S. M., Majila, K., & Viswanath, S. (2025) · Springer handbooks · doi:10.1007/978-3-031-81728-1_47 · Cited by 7

Artificial intelligence in cryo-EM: emerging deep neural network methods from sample preparation, particle picking, map reconstruction, modelling to enhanced resolution

Iqbal, S., Eng, E. T., Kamal, M. A., & Shen, B. (2026) · BMC Artificial Intelligence · doi:10.1186/s44398-025-00017-2 · Cited by 3

Advances in Crystallography and Cryo-Electron Microscopy for the Study of Membrane Proteins

Megta, A. K., Punetha, A., Kumari, J., Wei, H., Rosario-Garrido, S., Tranos, J. A., & Petrou, V. I. (2026) · Advances in experimental medicine and biology · doi:10.1007/978-3-032-07523-9_4 · Cited by 2

Cytochrome nanowires under electron microscopy

Petersen, H. A., Hochbaum, A. I., Bond, D. R., & Wang, F. (2026) · Emerging Topics in Life Sciences · doi:10.1042/etls20240008 · Cited by 2

Structures of Photosynthetic Supramolecular Complexes

Liu, Z., Wang, Y. X., Li, M., & Sui, S.-F. (2026) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-021424-011156 · Cited by 2

Plant structural biology: Emerging technologies and future biological insights

Böhm, J. M., & Maurino, V. G. (2026) · The Plant Journal · doi:10.1111/tpj.70786 · Cited by 2

A Visualization Tool for Cryo-EM Protein Validation with an Unsupervised Machine Learning Model in Chimera Platform

Chen, L., Baker, B., Santos, E., Sheep, M., & Daftarian, D. (2019) · Medicines · doi:10.3390/medicines6030086 · Cited by 2

Across scales: novel insights into kidney health and disease by structural biology

Tomas, N. M., Mortensen, S. A., Wilmanns, M., & Huber, T. B. (2021) · Kidney International · doi:10.1016/j.kint.2021.03.042 · Cited by 2

Cryo-EM structure of a single-chain β1-adrenoceptor – AmpC β-lactamase fusion protein

Collu, G., Mohammed, I., Lafita, A., Bierig, T., Poghosyan, E., Bliven, S. E., Rabl, J., Afanasyev, P., & Benoit, R. (2026) · Journal of Structural Biology · doi:10.1016/j.jsb.2026.108349 · Cited by 2

Remarkable interfacial dielectric relaxation of physically cross-linked ice-hydrogelRemarkable interfacial dielectric relaxation of physically cross-linked ice-hydrogel

Li, Y., Zhai, W., Liu, B., Li, C., Lin, L., Yan, Z. B., Jiang, X., Liu, W., & Liu, J. (2021) · Soft Science · doi:10.20517/ss.2021.13 · Cited by 2

CryoEM analysis of small plant biocatalysts at sub-2 Å resolution

Dimos, N., Helmer, C. P. O., Chánique, A. M., Wahl, M. C., Kourist, R., Hilal, T., & Loll, B. (2021) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s205979832101216x · Cited by 2

CryoEM analysis of small plant biocatalysts at sub-2 Å resolution

Dimos, N., Helmer, C. P. O., Chánique, A. M., Wahl, M. C., Kourist, R., Hilal, T., & Loll, B. (2022) · HZB Repository (Helmholtz-Zentrum Berlin für Materialien und Energie GmbH (HZB)) · doi:10.17169/refubium-33042 · Cited by 2

Structures of multisubunit membrane complexes with the CRYO ARM 200

Gerle, C., Kishikawa, J.-I., Yamaguchi, T., Nakanishi, A., Çoruh, O., Makino, F., Miyata, T., Kawamoto, A., Yokoyama, K., Namba, K., et al. (2022) · Microscopy · doi:10.1093/jmicro/dfac037 · Cited by 2

Capturing membrane structure and function in lattice Boltzmann models

McClure, J. E., & Li, Z. (2023) · Physical review. E · doi:10.1103/physreve.107.024408 · Cited by 2

SegmA: Residue Segmentation of cryo-EM density maps

Rozanov, M., & Wolfson, H. J. (2023) · IEEE International Conference on Bioinformatics and Biomedicine (BIBM) · doi:10.1109/bibm58861.2023.10385980 · Cited by 2

Deep neural-network prior for orbit recovery from method of moments

Khoo, Y., Paul, S., & Sharon, N. (2024) · Journal of Computational and Applied Mathematics · doi:10.1016/j.cam.2024.115782 · Cited by 2

Exploring advances in single particle CryoEM with apoferritin: From blobs to true atomic resolution

Premageetha, G. T. R., Vinothkumar, K. R., & Bose, S. (2024) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2024.106536 · Cited by 2

Analysis of the Conformational Landscape of the N-Domains of the AAA ATPase p97: Disentangling the Continuous Conformational Variability in Partially Symmetrical Complexes

Valimehr, S., Vuillemot, R., Kazemi, M., Jonić, S., & Rouiller, I. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25063371 · Cited by 2

Development of silicon-on-insulator direct electron detector with analog memories in pixels for sub-microsecond imaging

Ishida, T., Sugie, K., Miyoshi, T., Ishida, Y., Saitoh, K., Arai, Y., & Kuwahara, M. (2024) · Microscopy · doi:10.1093/jmicro/dfae029 · Cited by 2

Semantic segmentation-based detection algorithm for challenging cryo-electron microscopy RNP samples

Vargas, J., Modrego, A., Canabal, H. A., & Martín‐Benito, J. (2024) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2024.1473609 · Cited by 2

Four decades of Eukaryotic DNA replication: From yeast genetics to high-resolution cryo-EM structures of the replisome

Tye, B. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2415231121 · Cited by 2

DNA Nanotags for Multiplexed Single-Particle Electron Microscopy and In Situ Electron Cryotomography

Chen, Y., Huang, Y., & Yang, Y. R. (2024) · JACS Au · doi:10.1021/jacsau.4c00986 · Cited by 2

A novel "bio-tag" for cryo-EM studies based on the small, electron-dense protein Csp1

Yao, W., Oken, A. C., & Farrens, D. (2025) · Biophysical Journal · doi:10.1016/j.bpj.2025.03.018 · Cited by 2

The Growing Role of Electron Microscopy in Anti-parasitic Drug Discovery

Johnson, R. M., Rawson, S., McPhillie, M. J., Fishwick, C. W. G., & Muench, S. P. (2018) · Current Medicinal Chemistry · doi:10.2174/0929867324666171109120526 · Cited by 2

Von der Elektronenkristallographie zur Einzelpartikel‐KryoEM (Nobel‐Aufsatz)

Henderson, R. A. (2018) · Angewandte Chemie · doi:10.1002/ange.201802731 · Cited by 2

Structure and supramolecular architecture of chloroplast ATP synthase

Minges, A., & Groth, G. (2020) · Advances in botanical research · doi:10.1016/bs.abr.2020.07.004 · Cited by 3

Quantitative phase imaging of single particles from a cryoEM micrograph

Pant, A., Banerjee, M., & Khare, K. (2021) · Optics Communications · doi:10.1016/j.optcom.2021.127588 · Cited by 2

The Use of Amphipols for Electron Microscopy

Popot, J. (2018) · Biological and medical physics, biomedical engineering · doi:10.1007/978-3-319-73148-3_12 · Cited by 2

X-Ray Tomography

Jacobsen, C. J. (2019) · Cambridge University Press eBooks · doi:10.1017/9781139924542.009 · Cited by 2

Large-scale Parallel Design for Cryo-EM Structure Determination on Heterogeneous Many-core Architectures

Qiao, L., Yu, H., Wang, K., Sun, R., Zhao, W., Fu, H., & Yang, G. (2019) · IEEE International Conference on Bioinformatics and Biomedicine (BIBM) · doi:10.1109/bibm47256.2019.8983081 · Cited by 2

Radiation Damage and Cryo Microscopy

Jacobsen, C. J. (2019) · Cambridge University Press eBooks · doi:10.1017/9781139924542.012 · Cited by 2

A resolution record for cryoEM

Ashmore, J. F., Carragher, B. O., Rosenthal, P. B., & Weis, W. I. (2021) · Faculty Reviews · doi:10.12703/r-01-000002 · Cited by 2

A Novel Event-Based Active Pixel Sensor for Cryo-EM Electron Counting

Bammes, B. E., & Bilhorn, R. B. (2021) · Microscopy and Microanalysis · doi:10.1017/s1431927621004979 · Cited by 2

Generative Adversarial Networks for Robust Cryo-EM Image Denoising

Gu, H., Xian, Y., Unarta, I. C., & Yao, Y. (2022) · Springer eBooks · doi:10.1007/978-3-030-03009-4_126-1 · Cited by 2

Algorithms and programs for the shell decomposition of oscillating functions in space

Urzhumtseva, L., Lunin, V. Y., & Urzhumtsev, A. (2022) · Journal of Applied Crystallography · doi:10.1107/s160057672201144x · Cited by 6

In the Age of Machine Learning Cryo‐EM Research is Still Necessary: A Path toward Precision Medicine

Stephens, D. C., Crabtree, A., Beasley, H. K., Lopez, E. G., Mungai, M., Vang, L., Neikirk, K., Vue, Z., Vue, N., Marshall, A. G., et al. (2023) · Advanced Biology · doi:10.1002/adbi.202300122 · Cited by 2

Ethoxylate Polymer-Based 96-Well Screen for Protein Crystallization

Demmer, U., Lemaire, O. N., Belhamri, M., & Ermler, U. (2023) · Crystals · doi:10.3390/cryst13101519 · Cited by 2

EMhub: a web platform for data management and on-the-fly processing in scientific facilities

de la Rosa-Trevin, J. M., Sharov, G., Fleischmann, S., Morado, D. R., Bollinger, J. C., Miller, D. J., Terry, D. S., Blanchard, S. C., Fernández, I. S., & Carroni, M. (2024) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798324009471 · Cited by 2

Nuclear Magnetic Resonance Techniques for the Study of Glycan Interactions

Atxabal, U., Gimeno, A., & Jiménez‐Barbero, J. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-819475-1.00015-8 · Cited by 2

Single Particle Analysis for High-Resolution 2D Electron Crystallography

Righetto, R. D., & Stahlberg, H. (2020) · Methods in molecular biology · doi:10.1007/978-1-0716-0966-8_12 · Cited by 2

2D Electron Crystallography of Membrane Protein Single-, Double-, and Multi-Layered Ordered Arrays

Johnson, M. C., Uddin, Y. M., Neselu, K., & Schmidt‐Krey, I. (2020) · Methods in molecular biology · doi:10.1007/978-1-0716-0966-8_10 · Cited by 2

Engineering Crystal Packing in RNA-Protein Complexes II: A Historical Perspective from the Structural Studies of the Spliceosome

Leung, A. K.-W., Kondo, Y., Krummel, D. P., Li, J., Price, S. R., & van Roon, A. M. (2021) · Crystals · doi:10.3390/cryst11080948 · Cited by 2

A recurring packing contact in crystals of InlB pinpoints functional binding sites in the internalin domain and the B repeat

Geerds, C., Bleymüller, W. M., Meyer, T., Widmann, C., & Niemann, H. H. (2022) · Desy publication database (The Deutsches Elektronen-Synchrotron) · Cited by 2

TopoStats – a program for automated tracing of biomolecules from AFM imagesPreprint

Beton, J. G., Moorehead, R., Helfmann, L., Gray, R., Hoogenboom, B. W., Joseph, A. P., Topf, M., & Pyne, A. L. B. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.09.23.309609 · Cited by 2

Robust Denoising of Cryo-EM Images via β-GANPreprint

Gu, H., Unarta, I. C., Huang, X., & Yao, Y. (2021) · Research Square · doi:10.21203/rs.3.rs-139567/v1 · Cited by 2

A versatile protocol for purifying recombinant proteins from Nicotiana benthamiana for structural studiesPreprint

Lawson, A. W., Macha, A., Neumann, U., Gunkel, M., Chai, J., Behrmann, E., & Schulze‐Lefert, P. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.10.13.618061 · Cited by 2

Cryogenic light microscopy of vitrified samples with Ångstrom precisionPreprint

Mazal, H., Wieser, F.-F., Bollschweiler, D., & Sandoghdar, V. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.05.27.656160 · Cited by 2

Microsecond Time-Resolved Cryo-EM Based on Jet VitrificationPreprint

Haubner, M., Williams, H. M., Hruby, J., Straub, M. S., Guskov, A., Kovalev, K., Drabbels, M., & Lorenz, U. J. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.11.21.689681 · Cited by 3

Azimuthal Segment Imaging in cryo-STEM TomographyPreprint

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