ReviewInternational journal of molecular sciences2019
Structure Determination by Single-Particle Cryo-Electron Microscopy: Only the Sky (and Intrinsic Disorder) is the Limit.
Review in International journal of molecular sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed.
- Label-free optical observation of disordered-to-ordered transitions in single intrinsically disordered proteins.Npj biosensing · 2026Article
- Cryo-EM single-particle analysis expanding towards increasingly native samples.Acta crystallographica. Section D, Structural biology · 2025Review
- Sensing Protein Structural Transitions with Microfluidic Modulation Infrared Spectroscopy.Biosensors · 2025Article
- Integrating chemical artificial intelligence and cognitive computing for predictive analysis of biological pathways: a case for intrinsically disordered proteins.Biophysical reviews · 2025Review
- A Simple Protocol for Visualization of RNA-Protein Complexes by Atomic Force Microscopy.Current protocols · 2025Article
- Navigating the unstructured by evaluating alphafold's efficacy in predicting missing residues and structural disorder in proteins.PloS one · 2025Article
- An integrative structural study of the human full-length RAD52 at 2.2 Å resolution.Communications biology · 2024Article
- Identifying protein conformational states in the Protein Data Bank: Toward unlocking the potential of integrative dynamics studies.Structural dynamics (Melville, N.Y.) · 2024Article
- The application and development of electron microscopy for three-dimensional reconstruction in life science: a review.Cell and tissue research · 2024Review
- Insights into protein structure using cryogenic light microscopy.Biochemical Society transactions · 2023Review
- Local Disordered Region Sampling (LDRS) for ensemble modeling of proteins with experimentally undetermined or low confidence prediction segments.Bioinformatics (Oxford, England) · 2023Article
- Local Disordered Region Sampling (LDRS) for Ensemble Modeling of Proteins with Experimentally Undetermined or Low Confidence Prediction Segments.bioRxiv : the preprint server for biology · 2023Article
- Role of surfactants in electron cryo-microscopy film preparation.Biophysical journal · 2023Article
- Potassium Ion Channels in Glioma: From Basic Knowledge into Therapeutic Applications.Membranes · 2023Review
- Lessons Learnt from COVID-19: Computational Strategies for Facing Present and Future Pandemics.International journal of molecular sciences · 2023Review
- Illuminating Intrinsically Disordered Proteins with Integrative Structural Biology.Biomolecules · 2023Review
- NMR insights into dynamic, multivalent interactions of intrinsically disordered regions: from discrete complexes to condensates.Essays in biochemistry · 2022Article
- Characterization of conformational heterogeneity via higher-dimensionality, proton-detected solid-state NMR.Journal of biomolecular NMR · 2022Article
- Intrinsically Disordered Proteins: An Overview.International journal of molecular sciences · 2022Review
- Linear discriminant analysis reveals hidden patterns in NMR chemical shifts of intrinsically disordered proteins.PLoS computational biology · 2022Article
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Traditionally, X-ray crystallography and NMR spectroscopy represent major workhorses of structural biologists, with the lion share of protein structures reported in protein data bank (PDB) being generated by these powerful techniques. Despite their wide utilization in protein structure determination, these two techniques have logical limitations, with X-ray crystallography being unsuitable for the analysis of highly dynamic structures and with NMR spectroscopy being restricted to the analysis of relatively small proteins. In recent years, we have witnessed an explosive development of the techniques based on Cryo-electron microscopy (Cryo-EM) for structural characterization of biological molecules. In fact, single-particle Cryo-EM is a special niche as it is a technique of choice for the structural analysis of large, structurally heterogeneous, and dynamic complexes. Here, sub-nanometer atomic resolution can be achieved (i.e., resolution below 10 Å) via single-particle imaging of non-crystalline specimens, with accurate 3D reconstruction being generated based on the computational averaging of multiple 2D projection images of the same particle that was frozen rapidly in solution. We provide here a brief overview of single-particle Cryo-EM and show how Cryo-EM has revolutionized structural investigations of membrane proteins. We also show that the presence of intrinsically disordered or flexible regions in a target protein represents one of the major limitations of this promising technique.
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