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https://www.rcsb.org/structure/7WOT
RCSB PDB - 7WOT: Cryo-EM structure of the inner ring monomer of the Saccharomyces cerevisiae...
Cryo-EM structure of the inner ring monomer of the Saccharomyces cerevisiae nuclear pore complex
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https://empiar.pdbj.org/zh-hant/entry/11680/
EMPIAR-11680 - Single particle cryo-EM dataset of sarkosyl-insoluble fraction from tg-SwDI mouse...
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https://www.rcsb.org/structure/9LRC
RCSB PDB - 9LRC: Cryo-EM structure of the histamine H4 receptor-Gi protein complex (Receptor...
Cryo-EM structure of the histamine H4 receptor-Gi protein complex (Receptor focused)
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https://cryo-em.hkust.edu.hk/bwg_gallery/workshopsymposium/
Workshop&Symposium – Cryo-EM facility
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https://www.thermofisher.com/blog/atomic-resolution/targeted-protein-degradation-novel-therapeutic-for-undruggable-targets/
Targeted Protein Degradation - Cryo EM - Undruggable Targets
Mar 10, 2026 - Learn how cryo-EM supports the development of small molecule drugs for targeted protein degradation of previously undruggable diseases.
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https://cci.lbl.gov/ceres/table_all/12_2024/?page=1&sort=-cbetadev
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https://pncc.labworks.org/training/dataprocess/beta
Data Processing (BETA) | Pacific Northwest Center for Cryo-EM
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https://cci.lbl.gov/ceres/table_all/08_2025/?page=1&sort=rota_outliers
cryo-EM Re-Refine
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https://cci.lbl.gov/ceres/table_all/00_0000/?sort=n_atoms&page=2
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https://cci.lbl.gov/ceres/table_all/02_2025/?sort=-pdb_code_mod&page=5
cryo-EM Re-Refine
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https://plantcmb.wisc.edu/event/gisriel-lab-2/
Gisriel lab: Chris Brininger – Cryo-EM Structures of Photosystem I with Alternative Quinones...
Studying the fundamental mechanisms of plant biology
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https://cci.lbl.gov/ceres/table_success/09_2023/?sort=-bond_mean&page=2
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https://empiar.pdbj.org/zh-hant/entry/10770/
EMPIAR-10770 - Cryo-EM reveals the stochastic nature of individual ATP binding events in a group II...
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https://womeninscience.ucsf.edu/publications/cryo-em-structures-reveal-dramatic-remodeling-p97-hexamer-multi-domain-adapter-ubxd1
Cryo-EM structures reveal dramatic remodeling of the p97 hexamer by the multi-domain adapter UBXD1....
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https://cci.lbl.gov/ceres/table_success/06_2026/?sort=r_min_nonbonded&page=2
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https://cci.lbl.gov/ceres/table_all/03_2025/?page=2&sort=-r_rama_outliers
cryo-EM Re-Refine
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https://www.protochips.com/blog/how-to-achieve-superior-cryo-em-application-results/
How to Achieve Superior Cryo-EM Application Results - Protochips
Mar 1, 2025 - Introduction Cryo-electron microscopy (cryo-EM) is a form of transmission electron microscopy (TEM) based on the principle of cryogenically freezing biological...
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https://cci.lbl.gov/ceres/table_all/11_2024/?sort=d_model
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https://cci.lbl.gov/ceres/table_all/01_2023/?sort=angle_mean
cryo-EM Re-Refine
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https://liner.com/review/improving-abinitio-cryoem-reconstruction-with-semiamortized-pose-inference
Improving Ab-Initio Cryo-EM Reconstruction with Semi-Amortized Pose Inference [Quick Review]
Regarding this NeurIPS 2024 paper, this review summarizes CryoSPIN, a semi-amortized method improving cryo-EM reconstruction quality and pose inference.
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https://cci.lbl.gov/ceres/table_all/06_2025/?sort=r_dihe_mean&page=3
cryo-EM Re-Refine
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https://www.ncbi.nlm.nih.gov/Structure/pdb/7OK0
7OK0: Cryo-EM structure of the Sulfolobus acidocaldarius RNA polymerase at 2.88 A
Conserved proteinDNA-directed RNA polymerase subunit A'DNA-directed RNA polymerase subunit A''DNA-directed RNA polymerase subunit BDNA-directed RNA polymerase...
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https://www2.rcsb.org/news/6679793750bece1b815a1450
Paper Published: Cryo-EM Ligand Modeling Challenge
Results of the 2021 Challenge and recommendations for best practices for assessing cryo-EM structures of liganded macromolecules reported at near-atomic...
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https://media.malayansaintifika.id/articles/2
Struktur Cryo-EM FANCJ Ungkap Mekanisme Pembukaan G-Quadrupleks dan Mutasi Terkait Penyakit ·...
Protein FANCJ merupakan helikase yang bertanggung jawab membuka struktur G‑quadrupleks pada DNA, dan gangguan pada fungsinya dikaitkan dengan anemia Fanconi...
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https://cci.lbl.gov/ceres/table_all/09_2024/?page=2&sort=r_chir_mean
cryo-EM Re-Refine
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https://dr.iiserpune.ac.in/items/be6cb46d-4571-4d74-ad9d-76517ff47bc0
Megabody Scaffold Constructs as tools for Cryo-EM structure determination and novel purification...
Cryo-EM structure determination currently faces several challenges when it comes to imaging and analysis of smaller proteins. Preferred orientation bias and...
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https://empiar.pdbj.org/ko/entry/12229/
EMPIAR-12229 - Cryo-EM structure of in-vitro alpha-synuclein fibril [5193 multi-frame micrographs...
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https://cci.lbl.gov/ceres/table_all/08_2025/?page=3&sort=-r_rama_allowed
cryo-EM Re-Refine
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https://www.ccp4.ac.uk/job/postdoctoral-position-in-cryo-em-at-lmb-in-jan-lowes-group/
postdoctoral position in cryo-EM at LMB in Jan Löwe’s group – Collaborative Computational Project...
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https://cci.lbl.gov/ceres/table_all/09_2024/?sort=r_d_model&page=5
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https://semmelweisinstitute.ac.at/june-semmelweis-seminar-cryo-em-specialist-andrew-ward/
June Semmelweis Seminar: Cryo-EM specialist Andrew Ward - the Ignaz Semmelweis Institute
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https://www.ncbi.nlm.nih.gov/Structure/pdb/8T5D
8T5D: Cryo-EM studies of the interplay between uS2 ribosomal protein and leaderless mRNA during...
16s RNA23S RNA30S ribosomal protein S1030S ribosomal protein S1130S ribosomal protein S1230S ribosomal protein S1330S ribosomal protein S1430S ribosomal...
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https://cci.lbl.gov/ceres/table_all/07_2023/?sort=r_angle_mean
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https://cci.lbl.gov/ceres/table_all/08_2025/?sort=n_residues&page=2
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https://www.helixbiostructures.com/publications/cryo-em-structures-of-pp2a-b55-fam122a-and-pp2a-b55-arpp19
Publication: Cryo-EM structures of PP2A:B55–FAM122A and PP2A:B55–ARPP19
Cryo-EM structures of PP2A:B55 with ARPP19 and FAM122A reveal unique binding mechanisms, shedding light on mitotic regulation and potential therapeutic targets.
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https://www.incb018424.com/index.php?g=Wap&m=Article&a=detail&id=448
HCAR3 Agonist Selectivity: Cryo-EM Insights – Inhibitor Research Hub
HCAR3 Agonist Selectivity: Cryo-EM Insights Hydroxycarboxylic acid receptors are metabolite-sensing G-protein-coupled receptors with important roles in li
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https://www.vita-journal.com/vita/EN/10.15302/vita.2026.04.0030
Hierarchical assembly of native cytoplasmic lattices revealed by cryo-EM
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https://cci.lbl.gov/ceres/table_all/09_2024/?page=4&sort=dihe_mean
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https://cryoem.wisc.edu/mccet-protocols/
MCCET Protocols — Coming Soon!! – UW-Madison Cryo-EM Research Center – UW–Madison
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https://pdbj.org/emnavi/quick.php?id=pdb-32fd
PDB-32fd: Cryo-EM structure of cariprazine-bound D3 dopamine receptor with ... - Yorodumi
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https://www.bbmb.iastate.edu/event/2024/bbmb-seminar-greg-martin-assistant-professor-iowa-state-university-beyond-rtss-how-cryo
BBMB Seminar - Greg Martin, Assistant Professor, Iowa State University; Beyond RTS,S: How cryo-EM...
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https://www.ncbi.nlm.nih.gov/Structure/pdb/5A1Z
5A1Z: Cryo-EM structure of Dengue virus serotype 2 strain PVP94-07 complexed with human antibody...
ANTIGEN-BINDING FRAGMENT OF HUMAN ANTIBODY 2D22 - HEAVY CHAINANTIGEN-BINDING FRAGMENT OF HUMAN ANTIBODY 2D22 - LIGHT CHAINENVELOPE PROTEINMEMBRANE GLYCOPROTEIN
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https://cci.lbl.gov/ceres/table_all/09_2025/?sort=d99&page=3
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https://dspace.mit.edu/entities/publication/c013338d-ae3d-4a14-a803-6727afbc4ae4
Uncovering structural ensembles from single-particle cryo-EM data using cryoDRGN
Single-particle cryogenic electron microscopy (cryo-EM) has emerged as a powerful technique to visualize the structural landscape sampled by a protein complex....
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https://www.ncbi.nlm.nih.gov/Structure/pdb/8SGH
8SGH: Cryo-EM structure of Karyopherin-beta2 bound to HNRNPH2 PY-NLS
Heterogeneous nuclear ribonucleoprotein H2, N-terminally processedTransportin-1
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https://www.ncbi.nlm.nih.gov/Structure/pdb/9BGE
9BGE: Cryo-EM structure of mAb8-24 bound to 426c.WITO.TM.SOSIP
426c.WITO.TM.SOSIPFv domain of heavy chain of mAb 8-24Fv domain of light chain of mAb...
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https://profiles.umassmed.edu/display/18889915
Atomic Resolution Cryo-EM Structure of ?-Galactosidase. | Profiles RNS
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https://cci.lbl.gov/ceres/table_fail/10_2023/?sort=plan_mean
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https://cryoem.world/
One World Cryo-EM – Algorithms and Computational Methods for Cryo-EM
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https://www.rcsb.org/structure/9OMG
RCSB PDB - 9OMG: Cryo-EM structure of rhesus antibody V033-a.I1 in complex with HIV Env trimer...
Cryo-EM structure of rhesus antibody V033-a.I1 in complex with HIV Env trimer Q23.17 MD39
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https://empiar.pdbj.org/ja/entry/13175/
EMPIAR-13175 - Single-particle cryo-EM data of Apo ReChb [27453 multi-frame micrographs composed of...
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https://www.ncbi.nlm.nih.gov/Structure/pdb/8ZXP
8ZXP: Cryo-EM structure of TmaT-TMA complexes
Trimethylamine transporterN,N-dimethylmethanamine
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https://edoc.mdc-berlin.de/id/eprint/26659/
Cryo-EM structure of the naked mole-rat ribosome reveals a stabilized split 28S rRNA - MDC...
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https://cci.lbl.gov/ceres/table_fail/08_2025/?sort=-r_rota_outliers&page=2
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https://www.rcsb.org/structure/6AH3
RCSB PDB - 6AH3: Cryo-EM structure of yeast Ribonuclease P with pre-tRNA substrate
Cryo-EM structure of yeast Ribonuclease P with pre-tRNA substrate
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https://cci.lbl.gov/ceres/table_success/08_2025/?sort=clashscore
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https://www.truecoursebio.com/about/news/cryo-em-incites-a-resolution-revolution-rousing-drug-discovery
Cryo-EM Resolution Revolution at NanoImaging Services
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https://cci.lbl.gov/ceres/table_success/09_2024/?sort=-date_from_header&page=2
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https://cris.ariel.ac.il/ar/publications/apple-picker-automatic-particle-picking-a-low-effort-cryo-em-fram-3/fingerprints/
APPLE picker: Automatic particle picking, a low-effort cryo-EM framework - بصمة -
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https://pdbj.org/emnavi/quick.php?id=EMD-25787
EMDB-25787: C2-symmetric single-particle cryo-EM map of T. vaginalis FDPF3 - Yorodumi
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https://cci.lbl.gov/ceres/table_fail/12_2025/?sort=cbetadev
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https://aluminium.atomistry.com/pdb9f20.html
Aluminium in PDB 9f20: Cryo-Em Structure of the I923V MDA5-Dsrna Filament with Adp-ALF4 Bound and...
Aluminium in PDB 9f20: Cryo-Em Structure of the I923V MDA5-Dsrna Filament with Adp-ALF4 Bound and 88-Degree Helical Twist
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https://cci.lbl.gov/ceres/table_fail/03_2024/?sort=rama_outliers
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https://cci.lbl.gov/ceres/table_success/02_2025/?sort=bond_mean&page=4
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https://cci.lbl.gov/ceres/table_all/08_2025/?sort=r_rama_favored
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https://cosmic-cryoem.org/single-particle-cryo-em-tools/
Single particle cryo-EM tools – COSMIC2
Apr 5, 2023 - We offer single particle cryo-EM software for analyzing stacks of extracted particles. At the moment, we do not offer end-to-end single particle analysis...
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https://cci.lbl.gov/ceres/table_all/09_2024/?page=3&sort=-map_code_str
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https://cci.lbl.gov/ceres/table_success/06_2026/?sort=r_angle_mean&page=2
cryo-EM Re-Refine
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https://cci.lbl.gov/ceres/table_all/12_2025/?sort=r_min_nonbonded
cryo-EM Re-Refine
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https://www.rcsb.org/structure/8IU2
RCSB PDB - 8IU2: Cryo-EM structure of Long-wave-sensitive opsin 1
Cryo-EM structure of Long-wave-sensitive opsin 1
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https://www.manufacturingchemist.com/fairjourney-bio-cryo-em-services-antibody-discovery-design
FairJourney Bio launches cryo-EM services to support antibody discovery and biologics design
The new offering at the company's San Diego laboratories provides high-resolution structural insights to accelerate antibody discovery, selection and...
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https://www.rcsb.org/structure/8E3Y
RCSB PDB - 8E3Y: Cryo-EM structure of the VPAC1R-PACAP27-Gs complex
Cryo-EM structure of the VPAC1R-PACAP27-Gs complex
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https://cci.lbl.gov/ceres/table_fail/02_2025/?page=3&sort=r_z_score
cryo-EM Re-Refine
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https://cci.lbl.gov/ceres/table_success/09_2024/?sort=emringer&page=4
cryo-EM Re-Refine
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https://cci.lbl.gov/ceres/table_all/02_2025/?sort=n_water&page=5
cryo-EM Re-Refine
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https://analysisdoo.com/products/sample-vitrification-in-electron-microscopy/
Sample Vitrification for Cryo-EM | Analysis
Vitrification systems for cryo-electron microscopy sample preparation. Preserve native sample structure in amorphous ice for high-resolution structural
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https://www.quantifoil.com/resources/improve-cryo-em-sample-preparation-with-advice-from-the-experts-register
Webinar: Improve your cryo-EM sample preparation with advice from the experts
Together with EM Japan, Quantifoil held a Virtual Round Table on current methods in sample preparation for single-particle analysis in cryo-EM.
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