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

A Preparative Mass Spectrometer to Deposit Intact Large Native Protein Complexes

Fremdling, P., Esser, T. K., Saha, B., Makarov, A., Fort, K. L., Reinhardt-Szyba, M., Gault, J., & Rauschenbach, S. (2022) · ACS Nano · doi:10.1021/acsnano.2c04831 · Cited by 45

Better Cryo-EM Specimen Preparation: How to Deal with the Air–Water Interface?

Liu, N., & Wang, H. (2022) · Journal of Molecular Biology · doi:10.1016/j.jmb.2022.167926 · Cited by 42

New approaches towards the understanding of integral membrane proteins: A structural perspective on G protein‐coupled receptors

Grisshammer, R. (2017) · Protein Science · doi:10.1002/pro.3200 · Cited by 43

Structural Variability from Noisy Tomographic Projections

Andén, J., & Singer, A. (2018) · SIAM Journal on Imaging Sciences · doi:10.1137/17m1153509 · Cited by 40

Structural biology of G protein-coupled receptors: new opportunities from XFELs and cryoEM

Ishchenko, A., Gati, C., & Cherezov, V. (2018) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2018.03.009 · Cited by 42

19F NMR as a versatile tool to study membrane protein structure and dynamics

Rose-Sperling, D., Tran, M. A., Lauth, L. M., Goretzki, B., & Hellmich, U. A. (2019) · Biological Chemistry · doi:10.1515/hsz-2018-0473 · Cited by 42

Assessment of protein assembly prediction in CASP13

Guzenko, D., Lafita, A., Monastyrskyy, B., Kryshtafovych, A., & Duarte, J. M. (2019) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.25795 · Cited by 40

Molecular Pharmacology of P2X Receptors: Exploring Druggable Domains Revealed by Structural Biology

Oken, A. C., Krishnamurthy, I., Savage, J. C., Lisi, N. E., Godsey, M., & Mansoor, S. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.925880 · Cited by 41

Fully automatic macromolecular crystallography: the impact of MASSIF-1 on the optimum acquisition and quality of data

Bowler, M. W., Svensson, O., & Nurizzo, D. (2016) · Crystallography Reviews · doi:10.1080/0889311x.2016.1155050 · Cited by 41

Carbohydrate structure: the rocky road to automation

Agirre, J., Davies, G. J., Wilson, K. S., & Cowtan, K. D. (2016) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2016.11.011 · Cited by 42

Defining the hierarchical organisation of collagen VI microfibrils at nanometre to micrometre length scales

Godwin, A. R. F., Starborg, T., Sherratt, M. J., Roseman, A. M., & Baldock, C. (2016) · Acta Biomaterialia · doi:10.1016/j.actbio.2016.12.023 · Cited by 41

Know your detergents: A case study on detergent background in negative stain electron microscopy

Gewering, T., Januliene, D., Ries, A. B., & Moeller, A. (2018) · Journal of Structural Biology · doi:10.1016/j.jsb.2018.05.008 · Cited by 42

Cryo-EM structure of a functional monomeric Photosystem I from Thermosynechococcus elongatus reveals red chlorophyll cluster

Çoruh, O., Frank, A., Tanaka, H., Kawamoto, A., El-Mohsnawy, E., Kato, T., Namba, K., Gerle, C., Nowaczyk, M. M., & Kurisu, G. (2021) · Communications Biology · doi:10.1038/s42003-021-01808-9 · Cited by 41

Electron microscopy holdings of the Protein Data Bank: the impact of the resolution revolution, new validation tools, and implications for the future

Burley, S. K., Berman, H. M., Chiu, W., Dai, W., Flatt, J. W., Hudson, B. P., Kaelber, J. T., Khare, S. D., Kulczyk, A., Lawson, C. L., et al. (2022) · Biophysical Reviews · doi:10.1007/s12551-022-01013-w · Cited by 44

Processing of Cryo-EM Movie Data

Ripstein, Z. A., & Rubinstein, J. L. (2016) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2016.04.009 · Cited by 40

Toward Glycomaterials with Selectivity as Well as Affinity

Richards, S., & Gibson, M. I. (2021) · JACS Au · doi:10.1021/jacsau.1c00352 · Cited by 40

Structural biology: A golden era

Carugo, O., & Djinović‐Carugo, K. (2023) · PLoS Biology · doi:10.1371/journal.pbio.3002187 · Cited by 47

A minority of final stacks yields superior amplitude in single-particle cryo-EM

Zhu, J., Zhang, Q., Zhang, H., Shi, Z., Hu, M., & Bao, C. (2023) · Nature Communications · doi:10.1038/s41467-023-43555-x · Cited by 39

Advances in electron microscopy: A qualitative view of instrumentation development for macromolecular imaging and tomography

Schröder, R. R. (2015) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2015.05.010 · Cited by 39

(Cryo)Transmission Electron Microscopy of Phospholipid Model Membranes Interacting with Amphiphilic and Polyphilic Molecules

Meister, A., & Blume, A. (2017) · Polymers · doi:10.3390/polym9100521 · Cited by 39

The structure of TRPC ion channels

Li, J., Zhang, X., Song, X., Liu, R., Zhang, J., & Li, Z. (2019) · Cell Calcium · doi:10.1016/j.ceca.2019.03.005 · Cited by 39

Structural Perspectives on the Mechanism of Soluble Guanylate Cyclase Activation

Wittenborn, E. C., & Marletta, M. A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22115439 · Cited by 39

Ensemble Reweighting Using Cryo-EM Particle Images

Tang, W. S., Silva-Sánchez, D., Giraldo-Barreto, J., Carpenter, B., Hanson, S. M., Barnett, A. H., Thiede, E. H., & Cossio, P. (2023) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.3c01087 · Cited by 38

Single-particle electron microscopy in the study of membrane protein structure

Zorzi, R. D., Mi, W., Liao, M., & Walz, T. (2015) · Microscopy · doi:10.1093/jmicro/dfv058 · Cited by 40

The ribosome and its role in protein folding: looking through a magnifying glass

Javed, A., Christodoulou, J., Cabrita, L. D., & Orlova, E. V. (2017) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798317007446 · Cited by 41

Structural insights into the function of Elongator

Dalwadi, U., & Yip, C. K. (2018) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-018-2747-6 · Cited by 38

Classification of Single Particles from Human Cell Extract Reveals Distinct Structures

Verbeke, E. J., Mallam, A. L., Drew, K., Marcotte, E. M., & Taylor, D. W. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.06.022 · Cited by 36

SMA-PAGE: A new method to examine complexes of membrane proteins using SMALP nano-encapsulation and native gel electrophoresis

Pollock, N. L., Rai, M., Simon, K. S., Hesketh, S. J., Teo, A. C. K., Parmar, M., Sridhar, P., Collins, R. F., Lee, S. C., Stroud, Z., et al. (2019) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2019.05.011 · Cited by 38

In situ Microfluidic Cryofixation for Cryo Focused Ion Beam Milling and Cryo Electron Tomography

Fuest, M., Schaffer, M., Nocera, G. M., Galilea-Kleinsteuber, R. I., Messling, J., Heymann, M., Plitzko, J. M., & Burg, T. P. (2019) · Scientific Reports · doi:10.1038/s41598-019-55413-2 · Cited by 38

Changes in Membrane Protein Structural Biology

Birch, J., Cheruvara, H., Gamage, N., Harrison, P. J., Lithgo, R., & Quigley, A. (2020) · Biology · doi:10.3390/biology9110401 · Cited by 40

Structure of cyanobacterial photosystem I complexed with ferredoxin at 1.97 Å resolution

Li, J., Hamaoka, N., Makino, F., Kawamoto, A., Lin, Y., Rögner, M., Nowaczyk, M. M., Lee, Y., Namba, K., Gerle, C., et al. (2022) · Communications Biology · doi:10.1038/s42003-022-03926-4 · Cited by 37

Structural and functional diversity of Resistance-Nodulation-Division (RND) efflux pump transporters with implications for antimicrobial resistance

Kavanaugh, L. G., Dey, D., Shafer, W. M., & Conn, G. L. (2024) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00089-23 · Cited by 37

BioEM: GPU-accelerated computing of Bayesian inference of electron microscopy images

Cossio, P., Rohr, D., Baruffa, F., Rampp, M., Lindenstruth, V., & Hummer, G. (2016) · Computer Physics Communications · doi:10.1016/j.cpc.2016.09.014 · Cited by 37

Structures of biomolecular complexes by combination of NMR and cryoEM methods

Cuniasse, P., Tavares, P., Orlova, E. V., & Zinn‐Justin, S. (2017) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2016.12.008 · Cited by 40

Imaging of post-mortem human brain tissue using electron and X-ray microscopy

Lewis, A. J., Genoud, C., Pont, M., van de Berg, W. D. J., Frank, S., Stahlberg, H., Shahmoradian, S. H., & Al‐Amoudi, A. (2019) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2019.06.003 · Cited by 35

Cryo‐EM map interpretation and protein model‐building using iterative map segmentation

Terwilliger, T. C., Adams, P. D., Afonine, P. V., & Sobolev, O. V. (2019) · Protein Science · doi:10.1002/pro.3740 · Cited by 37

Recent advances in single-molecule fluorescence microscopy render structural biology dynamic

Bačić, L., Владимирович, С. А., & Deindl, S. (2020) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2020.05.006 · Cited by 36

The structure of the γ-TuRC: a 25-years-old molecular puzzle

Župa, E., Liu, P., Würtz, M., Schiebel, E., & Pfeffer, S. (2020) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2020.08.008 · Cited by 37

Forty years in cryoEM of membrane proteins

Kühlbrandt, W. (2021) · Microscopy · doi:10.1093/jmicro/dfab041 · Cited by 37

Community recommendations on cryoEM data archiving and validation

Kleywegt, G. J., Adams, P. D., Butcher, S. J., Lawson, C. L., Rohou, A. L., Rosenthal, P. B., Subramaniam, S., Topf, M., Abbott, S., Baldwin, P. R., et al. (2024) · IUCrJ · doi:10.1107/s2052252524001246 · Cited by 39

The cryo‐ EM structure of the Plasmodium falciparum 20S proteasome and its use in the fight against malaria

Li, H., Bogyo, M. S., & da Fonseca, P. C. A. (2016) · FEBS Journal · doi:10.1111/febs.13780 · Cited by 40

In Situ Imaging of Bacterial Secretion Systems by Electron Cryotomography

Weiss, G. L., Medeiros, J. M., & Pilhofer, M. (2017) · Methods in molecular biology · doi:10.1007/978-1-4939-7033-9_27 · Cited by 32

3D ab initio modeling in cryo-EM by autocorrelation analysis

Levin, E., Bendory, T., Boumal, N., Kileel, J., & Singer, A. (2018) · IEEE International Symposium on Biomedical Imaging (ISBI) · doi:10.1109/isbi.2018.8363873 · Cited by 36

Deep Learning for Validating and Estimating Resolution of Cryo-Electron Microscopy Density Maps †

Avramov, T. K., Vyenielo, D., Gómez-Blanco, J., Adinarayanan, S., Vargas, J., & Si, D. (2019) · Molecules · doi:10.3390/molecules24061181 · Cited by 36

Advances in Structure Modeling Methods for Cryo-Electron Microscopy Maps

Alnabati, E., & Kihara, D. (2019) · Molecules · doi:10.3390/molecules25010082 · Cited by 36

Opportunities and challenges for assigning cofactors in cryo-EM density maps of chlorophyll-containing proteins

Gisriel, C. J., Wang, J., Brudvig, G. W., & Bryant, D. A. (2020) · Communications Biology · doi:10.1038/s42003-020-01139-1 · Cited by 36

TEMPy2: a Python library with improved 3D electron microscopy density-fitting and validation workflows

Cragnolini, T., Sahota, H., Joseph, A., Sweeney, A., Malhotra, S., Vasishtan, D., & Topf, M. (2021) · Acta Crystallographica Section D: Structural Biology · doi:10.1107/s2059798320014928 · Cited by 31

Architecture of the polyketide synthase module: surprises from electron cryo-microscopy

Smith, J. L., Skiniotis, G., & Sherman, D. H. (2015) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2015.02.014 · Cited by 36

A posteriori correction of camera characteristics from large image data sets

Afanasyev, P., Ravelli, R. B. G., Matadeen, R., Carlo, S. D., van Duinen, G., Alewijnse, B., Peters, P. J., Abrahams, J. P., Portugal, R. V., Schatz, M. X., et al. (2015) · Scientific Reports · doi:10.1038/srep10317 · Cited by 35

Cryo-electron Microscopy Analysis of Structurally Heterogeneous Macromolecular Complexes

Jonić, S. (2016) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2016.10.002 · Cited by 37

RsgA couples the maturation state of the 30S ribosomal decoding center to activation of its GTPase pocket

López-Alonso, J. P., Kaminishi, T., Kikuchi, T., Hirata, Y., Iturrioz, I., Dhimole, N., Schedlbauer, A., Hase, Y., Goto, S., Kurita, D., et al. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx324 · Cited by 31

Advances in high-resolution cryo-EM of oligomeric enzymes

Vonck, J., & Mills, D. J. (2017) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2017.05.016 · Cited by 35

Structural biology of thermoTRPV channels

Yuan, P. (2019) · Cell Calcium · doi:10.1016/j.ceca.2019.102106 · Cited by 35

Cryo-EM structure of coronavirus-HKU1 haemagglutinin esterase reveals architectural changes arising from prolonged circulation in humans

Hurdiss, D. L., Drulyte, I., Lang, Y., Shamorkina, T. M., Pronker, M. F., van Kuppeveld, F. J. M., Snijder, J., & de Groot, R. J. (2020) · Nature Communications · doi:10.1038/s41467-020-18440-6 · Cited by 38

Cryomicroscopy in situ : what is the smallest molecule that can be directly identified without labels in a cell?

Russo, C. J., Dickerson, J. L., & Naydenova, K. (2022) · Faraday Discussions · doi:10.1039/d2fd00076h · Cited by 35

Artificial Intelligence in Cryo-Electron Microscopy

Chung, J. M., Durie, C. L., & Lee, J. (2022) · Life · doi:10.3390/life12081267 · Cited by 35

Viral Small Terminase: A Divergent Structural Framework for a Conserved Biological Function

Lokareddy, R. K., Hou, C.-F. D., Li, F., Yang, R., & Cingolani, G. (2022) · Viruses · doi:10.3390/v14102215 · Cited by 35

Single-particle cryo-electron microscopy of macromolecular complexes

Skiniotis, G., & Southworth, D. R. (2015) · Microscopy · doi:10.1093/jmicro/dfv366 · Cited by 35

Cryo-EM heterogeneity analysis using regularized covariance estimation and kernel regression

Gilles, M. A., & Singer, A. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2419140122 · Cited by 37

Bacterial cell envelope-targeting antibiotics

Ntallis, C., Martin, N. I., Edwards, A. M., & Weingarth, M. H. (2025) · Nature Reviews Microbiology · doi:10.1038/s41579-025-01247-x · Cited by 46

Tools for Model Building and Optimization into Near-Atomic Resolution Electron Cryo-Microscopy Density Maps

DiMaio, F., & Chiu, W. (2016) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2016.06.003 · Cited by 33

Evolving data standards for cryo-EM structures

Lawson, C. L., Berman, H. M., & Chiu, W. (2020) · Structural Dynamics · doi:10.1063/1.5138589 · Cited by 34

The rapidly evolving role of cryo-EM in drug design

Wigge, C., Stefanovic, A., & Radjainia, M. (2020) · Drug Discovery Today Technologies · doi:10.1016/j.ddtec.2020.12.003 · Cited by 33

Single-particle cryo-EM using alignment by classification (ABC): the structure ofLumbricus terrestrishaemoglobin

Afanasyev, P., Seer-Linnemayr, C., Ravelli, R. B. G., Matadeen, R., Carlo, S. D., Alewijnse, B., Portugal, R. V., Pannu, N. S., Schatz, M. X., & van Heel, M. (2017) · IUCrJ · doi:10.1107/s2052252517010922 · Cited by 33

ABC Transporters in Dynamic Macromolecular Assemblies

Trowitzsch, S., & Tampé, R. (2018) · Journal of Molecular Biology · doi:10.1016/j.jmb.2018.07.028 · Cited by 32

Using Scipion for stream image processing at Cryo-EM facilities

Gómez-Blanco, J., de la Rosa-Trevin, J. M., Marabini, R., del Caño, L., Jiménez, A., Martínez, M., Melero, R., Majtner, T., Maluenda, D., Mota, J., et al. (2018) · Journal of Structural Biology · doi:10.1016/j.jsb.2018.10.001 · Cited by 33

Methods for merging data sets in electron cryo-microscopy

Wilkinson, M. E., Kumar, A., & Casañal, A. (2019) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798319010519 · Cited by 33

Alternative conformations and motions adopted by 30S ribosomal subunits visualized by cryo-electron microscopy

Jahagirdar, D., Jha, V., Basu, K., Gómez-Blanco, J., Vargas, J., & Ortega, J. (2020) · RNA · doi:10.1261/rna.075846.120 · Cited by 33

Fake It ‘Till You Make It—The Pursuit of Suitable Membrane Mimetics for Membrane Protein Biophysics

Thoma, J., & Burmann, B. M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms22010050 · Cited by 40

StarMap: a user-friendly workflow for Rosetta-driven molecular structure refinement

Lugmayr, W., Kotov, V., Goessweiner‐Mohr, N., Wald, J., DiMaio, F., & Marlovits, T. C. (2022) · Nature Protocols · doi:10.1038/s41596-022-00757-9 · Cited by 33

Breaking the next Cryo-EM resolution barrier – Atomic resolution determination of proteins!Preprint

Yip, K. M., Fischer, N., Paknia, E., Chari, A., & Stark, H. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.05.21.106740 · Cited by 33

EMDA: A Python package for Electron Microscopy Data Analysis

Warshamanage, R., Yamashita, K., & Murshudov, G. N. (2021) · Journal of Structural Biology · doi:10.1016/j.jsb.2021.107826 · Cited by 33

‘Assembly and analysis of cell-scale membrane envelopes’

Vermaas, J. V., Mayne, C. G., Shinn, E., & Tajkhorshid, E. (2022) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.1c01050 · Cited by 30

Cryo-electron microscopy-based drug design

Cebi, E., Lee, J., Subramani, V. K., Bak, N., Oh, C., & Kim, K. K. (2024) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2024.1342179 · Cited by 34

Imaging bacteria inside their host by cryo-focused ion beam milling and electron cryotomography

Medeiros, J. M., Böck, D., & Pilhofer, M. (2017) · Current Opinion in Microbiology · doi:10.1016/j.mib.2017.12.006 · Cited by 32

Elucidating the structural basis for differing enzyme inhibitor potency by cryo-EM

Rawson, S. D., Bisson, C., Hurdiss, D. L., Fazal, A., McPhillie, M. J., Sedelnikova, S. E., Baker, P. J., Rice, D. W., & Muench, S. P. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1708839115 · Cited by 32

Calcium Channelopathies: Structural Insights into Disorders of the Muscle Excitation–Contraction Complex

Pancaroglu, R., & Petegem, F. V. (2018) · Annual Review of Genetics · doi:10.1146/annurev-genet-120417-031311 · Cited by 32

A Cyclometalated Iridium (III) Complex as a Microtubule Probe for Correlative Super‐Resolution Fluorescence and Electron Microscopy

Tian, X., Pace, C. D., Ruiz‐Pérez, L., Chen, B., Su, R., Zhang, M., Zhang, R., Zhang, Q., Wang, Q. L., Zhou, H., et al. (2020) · Advanced Materials · doi:10.1002/adma.202003901 · Cited by 32

Native Mass Spectrometry-Based Screening for Optimal Sample Preparation in Single-Particle Cryo-EM

Olinares, P. D. B., Kang, J. Y., Llewellyn, E., Chiu, C., Chen, J., Malone, B. F., Saecker, R. M., Campbell, E. A., Darst, S. A., & Chait, B. T. (2020) · Structure · doi:10.1016/j.str.2020.11.001 · Cited by 34

Evolution of standardization and dissemination of cryo-EM structures and data jointly by the community, PDB, and EMDB

Chiu, W., Schmid, M. F., Pintilie, G. D., & Lawson, C. L. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100560 · Cited by 32

Fully automated multi-grid cryoEM screening using Smart Leginon

Cheng, A., Kim, P. T., Kuang, H., Mendez, J. H., Chua, E. Y. D., Maruthi, K., Wei, H. A., Sawh-Gopal, A., Aragon, M. F., Serbynovskyi, V., et al. (2022) · IUCrJ · doi:10.1107/s2052252522010624 · Cited by 32

Application of the NZ‐1 Fab as a crystallization chaperone for PA tag‐inserted target proteins

Tamura, R., Oi, R., Akashi, S., Kaneko, M. K., Kato, Y., & Nogi, T. (2019) · Protein Science · doi:10.1002/pro.3580 · Cited by 31

Integrative biology of native cell extracts: a new era for structural characterization of life processes

Kyrilis, F. L., Meister, A., & Kastritis, P. L. (2019) · Biological Chemistry · doi:10.1515/hsz-2018-0445 · Cited by 31

Impact of the Protein Data Bank on antineoplastic approvals

Westbrook, J., Soskind, R., Hudson, B. P., & Burley, S. K. (2020) · Drug Discovery Today · doi:10.1016/j.drudis.2020.02.002 · Cited by 31

How structural biology transformed studies of transcription regulation

Wolberger, C. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100741 · Cited by 31

Iterative Molecular Dynamics–Rosetta Membrane Protein Structure Refinement Guided by Cryo-EM Densities

Leelananda, S. P., & Lindert, S. (2017) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.7b00464 · Cited by 31

Overview of Membrane Protein Sample Preparation for Single-Particle Cryo-Electron Microscopy Analysis

Vénien‐Bryan, C., & Fernandes, C. A. H. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241914785 · Cited by 30

Deciphering the molecular architecture of membrane contact sites by cryo-electron tomography

Collado, J., & Fernández‐Busnadiego, R. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2017.03.009 · Cited by 30

Revisiting the Structure of Hemoglobin and Myoglobin with Cryo-Electron Microscopy

Khoshouei, M., Danev, R., Plitzko, J. M., & Baumeister, W. P. (2017) · Journal of Molecular Biology · doi:10.1016/j.jmb.2017.07.004 · Cited by 30

Fluctuating Finite Element Analysis (FFEA): A continuum mechanics software tool for mesoscale simulation of biomolecules

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