ArticleThe journal of physical chemistry letters2020
Structural Heterogeneity in Single Particle Imaging Using X-ray Lasers.
Article in The journal of physical chemistry letters, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Biological applications at the AQUA beamline of the EuPRAXIA@SPARC_LAB free electron laser.European biophysics journal : EBJ · 2026Article
- Water layer and radiation damage effects on the orientation recovery of proteins in single-particle imaging at an X-ray free-electron laser.Scientific reports · 2023Article
- Rehydration Post-orientation: Investigating Field-Induced Structural Changes via Computational Rehydration.The protein journal · 2023Article
- Expected resolution limits of x-ray free-electron laser single-particle imaging for realistic source and detector properties.Structural dynamics (Melville, N.Y.) · 2022Article
- Article
- Stability and conformational memory of electrosprayed and rehydrated bacteriophage MS2 virus coat proteins.Current research in structural biology · 2022Article
- Charge Engineering Reveals the Roles of Ionizable Side Chains in Electrospray Ionization Mass Spectrometry.JACS Au · 2021Article
- Effects of radiation damage and inelastic scattering on single-particle imaging of hydrated proteins with an X-ray Free-Electron Laser.Scientific reports · 2021Article
- Protein orientation in time-dependent electric fields: orientation before destruction.Biophysical journal · 2021Article
- Reproducibility in the unfolding process of protein induced by an external electric field.Chemical science · 2020Article
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
One of the challenges facing single particle imaging with ultrafast X-ray pulses is the structural heterogeneity of the sample to be imaged. For the method to succeed with weakly scattering samples, the diffracted images from a large number of individual proteins need to be averaged. The more the individual proteins differ in structure, the lower the achievable resolution in the final reconstructed image. We use molecular dynamics to simulate two globular proteins in vacuum, fully desolvated as well as with two different solvation layers, at various temperatures. We calculate the diffraction patterns based on the simulations and evaluate the noise in the averaged patterns arising from the structural differences and the surrounding water. Our simulations show that the presence of a minimal water coverage with an average 3 Å thickness will stabilize the protein, reducing the noise associated with structural heterogeneity, whereas additional water will generate more background noise.
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