ReviewActa crystallographica. Section F, Structural biology communications2017
Cryo-electron microscopy and X-ray crystallography: complementary approaches to structural biology and drug discovery.
Review in Acta crystallographica. Section F, Structural biology communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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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.
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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.
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Who cites it
45 citing papers in PubMed.
- Exploration of the protein and pharmacological landscape of monkeypox virus treatment: from entry point to end point.Molecular diversity · 2026Review
- The evolving role of structural biology in pharma: integration of X-ray crystallography, cryo-electron microscopy and beyond.Acta crystallographica. Section D, Structural biology · 2026Review
- A Fivefold Maximum Drug-Likeness Strategy for Prioritizing Antibacterial Candidates AgainstPharmaceuticals (Basel, Switzerland) · 2026Article
- Protein structural dynamics in covalent drug design: insights from irreversible and reversible covalent inhibitors.RSC chemical biology · 2026Review
- Breaking barriers: transitioning from X-ray crystallography to cryo-EM for structural studies.Acta crystallographica. Section D, Structural biology · 2026Article
- Integrating deep learning with physics based modeling enables high precision antibody antigen interface prediction.Scientific reports · 2026Article
- Prediction of pre- and postfusion conformations of class I fusion proteins with AlphaFold2.PloS one · 2026Article
- Identification of Antibacterial Hits Associated with Penicillin-Binding Protein 2 inDrug design, development and therapy · 2026Article
- Beyond structures: solution NMR as the quantitative engine of integrated structural biology.Frontiers in molecular biosciences · 2026Review
- Breaking Barriers: Transitioning from X-ray Crystallography to Cryo-EM for Structural Studies of ATAD2B.bioRxiv : the preprint server for biology · 2025Article
- Resurgence of magnetic resonance techniques in the era of AlphaFold.Biophysical reviews · 2025Review
- Structural insights into Beclin 1 interactions with it's regulators for autophagy modulation.Computational and structural biotechnology journal · 2025Review
- Innovative Approaches in Molecular Docking for the Discovery of Novel Inhibitors Against Alzheimer's Disease.Current Alzheimer research · 2025Review
- AI-Driven Deep Learning Techniques in Protein Structure Prediction.International journal of molecular sciences · 2024Review
- Systematic computational strategies for identifying protein targets and lead discovery.RSC medicinal chemistry · 2024Review
- Expression, purification, and characterization of transmembrane protein homogentisate solanesyltransferase.Applied microbiology and biotechnology · 2024Article
- Cryo-electron microscopy-based drug design.Frontiers in molecular biosciences · 2024Review
- Advancements in small molecule drug design: A structural perspective.Drug discovery today · 2023Review
- Overview of Membrane Protein Sample Preparation for Single-Particle Cryo-Electron Microscopy Analysis.International journal of molecular sciences · 2023Review
- Potassium Ion Channels in Glioma: From Basic Knowledge into Therapeutic Applications.Membranes · 2023Review
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The invention of the electron microscope has greatly enhanced the view scientists have of small structural details. Since its implementation, this technology has undergone considerable evolution and the resolution that can be obtained for biological objects has been extended. In addition, the latest generation of cryo-electron microscopes equipped with direct electron detectors and software for the automated collection of images, in combination with the use of advanced image-analysis methods, has dramatically improved the performance of this technique in terms of resolution. While calculating a sub-10 Å resolution structure was an accomplishment less than a decade ago, it is now common to generate structures at sub-5 Å resolution and even better. It is becoming possible to relatively quickly obtain high-resolution structures of biological molecules, in particular large ones (>500 kDa) which, in some cases, have resisted more conventional methods such as X-ray crystallography or nuclear magnetic resonance (NMR). Such newly resolved structures may, for the first time, shed light on the precise mechanisms that are essential for cellular physiological processes. The ability to attain atomic resolution may support the development of new drugs that target these proteins, allowing medicinal chemists to understand the intimacy of the relationship between their molecules and targets. In addition, recent developments in cryo-electron microscopy combined with image analysis can provide unique information on the conformational variability of macromolecular complexes. Conformational flexibility of macromolecular complexes can be investigated using cryo-electron microscopy and multiconformation reconstruction methods. However, the biochemical quality of the sample remains the major bottleneck to routine cryo-electron microscopy-based determination of structures at very high resolution.
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