ReviewThe Journal of biological chemistry
Evolution of standardization and dissemination of cryo-EM structures and data jointly by the community, PDB, and EMDB.
Review in The Journal of biological chemistry. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
18 citing papers in PubMed.
- Incorporating targeted protein structure in deep learning methods for molecule generation in computational drug design.Chemical science · 2025Review
- Validation of helical symmetry parameters in the EMDB.Acta crystallographica. Section D, Structural biology · 2025Article
- Article
- A case for community metadata standards in cryo-electron tomography.Emerging topics in life sciences · 2025Review
- Preparation of oxygen-sensitive proteins for high-resolution cryoEM structure determination using blot-free vitrification.Nature communications · 2025Article
- Article
- Uncovering Protein Ensembles: Automated Multiconformer Model Building for X-ray Crystallography and Cryo-EM.bioRxiv : the preprint server for biology · 2024Article
- Scaling up cryo-EM for biology and chemistry: The journey from niche technology to mainstream method.Structure (London, England : 1993) · 2023Review
- UCSF ChimeraX: Tools for structure building and analysis.Protein science : a publication of the Protein Society · 2023Article
- Interaction of Vanadium Complexes with Proteins: Revisiting the Reported Structures in the Protein Data Bank (PDB) since 2015.Molecules (Basel, Switzerland) · 2023Review
- RCSB Protein Data Bank (RCSB.org): delivery of experimentally-determined PDB structures alongside one million computed structure models of proteins from artificial intelligence/machine learning.Nucleic acids research · 2023Article
- Using deep-learning predictions of inter-residue distances for model validation.Acta crystallographica. Section D, Structural biology · 2022Article
- Protein Data Bank: A Comprehensive Review of 3D Structure Holdings and Worldwide Utilization by Researchers, Educators, and Students.Biomolecules · 2022Review
- Imaging biological macromolecules in thick specimens: The role of inelastic scattering in cryoEM.Ultramicroscopy · 2022Article
- Better, Faster, Cheaper: Recent Advances in Cryo-Electron Microscopy.Annual review of biochemistry · 2022Review
- Structure of cytoplasmic ring of nuclear pore complex by integrative cryo-EM and AlphaFold.Science (New York, N.Y.) · 2022Article
- Complex Portal 2022: new curation frontiers.Nucleic acids research · 2022Article
- How the Protein Data Bank changed biology: An introduction to the JBC Reviews thematic series, part 1.The Journal of biological chemistryArticle
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
Abstract
Cryogenic electron microscopy (cryo-EM) methods began to be used in the mid-1970s to study thin and periodic arrays of proteins. Following a half-century of development in cryo-specimen preparation, instrumentation, data collection, data processing, and modeling software, cryo-EM has become a routine method for solving structures from large biological assemblies to small biomolecules at near to true atomic resolution. This review explores the critical roles played by the Protein Data Bank (PDB) and Electron Microscopy Data Bank (EMDB) in partnership with the community to develop the necessary infrastructure to archive cryo-EM maps and associated models. Public access to cryo-EM structure data has in turn facilitated better understanding of structure-function relationships and advancement of image processing and modeling tool development. The partnership between the global cryo-EM community and PDB and EMDB leadership has synergistically shaped the standards for metadata, one-stop deposition of maps and models, and validation metrics to assess the quality of cryo-EM structures. The advent of cryo-electron tomography (cryo-ET) for in situ molecular cell structures at a broad resolution range and their correlations with other imaging data introduce new data archival challenges in terms of data size and complexity in the years to come.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.