ReviewCurrent opinion in structural biology2019
CryoEM maps are full of potential.
Review in Current opinion in structural biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
43 citing papers in PubMed, 69 citations in OpenAlex.
- Predicting water at the protein interface in cryo-EM structures from MD-excess chemical potential.Biophysical journal · 2026Article
- Tracking the redox reaction of the iron enzyme ribonucleotide reductase using continuous SerialED and SFX.Structure (London, England : 1993) · 2026Article
- Quantum refinement with electron diffraction and X-ray free-electron laser data: comparative study of ribonucleotide reductase dimetal site.Journal of applied crystallography · 2026Article
- Article
- Direct evidence of acid-driven protein desolvation.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Direct from the seed: an atomic resolution protein structure by ab initio MicroED.Nature communications · 2026Article
- Cat_Wiz: a stereochemistry-guided toolkit for locating, diagnosing, and annotating Mg2+ ions in RNA structures.Nucleic acids research · 2026Article
- Article
- An Empirical Biasing Force Constant to Minimize Overfitting in Cryo-EM Flexible Fitting Refinement.Journal of chemical information and modeling · 2025Article
- Molecular basis of TRPV3 channel blockade by intracellular polyamines.Communications biology · 2025Article
- Comprehensive microcrystal electron diffraction sample preparation for cryo-EM.Nature protocols · 2025Review
- Cryo-EM analyses unveil details of mechanism and targocil-II mediated inhibition of S. aureus WTA transporter TarGH.Nature communications · 2025Article
- Advances in cryo-electron microscopy (cryoEM) for structure-based drug discovery.Expert opinion on drug discovery · 2025Review
- Connecting the dots: deep learning-based automated model building methods in cryo-EM.Frontiers in molecular biosciences · 2025Review
- Ligand identification in CryoEM and X-ray maps using deep learning.Bioinformatics (Oxford, England) · 2024Article
- Ligand Identification in CryoEM and X-ray Maps Using Deep Learning.bioRxiv : the preprint server for biology · 2024Article
- Structural biology and molecular pharmacology of voltage-gated ion channels.Nature reviews. Molecular cell biology · 2024Review
- Conformational changes in the Niemann-Pick type C1 protein NCR1 drive sterol translocation.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Role of Protonation States in the Stability of Molecular Dynamics Simulations of High-Resolution Membrane Protein Structures.The journal of physical chemistry. B · 2024Article
- Exploiting the full potential of cryo-EM maps.BBA advances · 2024Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
Electron microscopy is based on elastic scattering due to Coulomb forces between the incident electrons and the sample; thus, electron scattering is dependent on the charge distribution in the sample. Unlike atomic scattering factors for X-rays, electron scattering factors for some atoms are strongly dependent on scattering angle, and the scattering factor for ionic oxygen is negative at low scattering angle. This phenomenon can result in a significant negative contribution to Coulomb potential maps by oxygen and can result in deviations in the positions of positive map features from atomic centers. An important factor that can also complicate the interpretation of cryoEM maps is the exquisite sensitivity of macromolecules to damage from electron irradiation, especially the carboxylates of acidic amino acids. Ideally, when compared with electron density maps derived by X-ray crystallography, Coulomb potential maps can provide additional details about the electrostatic environment and charge state of atoms. Enhancements in model building, refinement and computational simulation will be required to realize the full potential of EM-derived maps to reveal deeper insight into the electronic structure and functional properties of macromolecular complexes and their interactions with binding partners, ligands, cofactors, and drugs.
Indexed as
Identifiers
What OpenQuestion holds
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.