bioRxiv Science⌕ Search

bioRxiv · 10.1101/2025.11.12.688030

Automated filtering of particle images in single particle cryoEM

Abstract

Continued exponential growth in the number of structures resolved by single particle cryoEM, as seen in the last decade, requires ever more effective data analysis workflows. Datasets are rarely homogeneous, demanding a multistep procedure for discarding outliers. Since individual particles are very noisy, either 2D or 3D averages are normally used for discrimination. This becomes challenging when the 2D classes themselves are heterogeneous, leading to selection of contaminants or discarding useful rare views/poses. The 3D model-based discrimination requires trustworthy 3D maps and a correct assignment of Euler angles, which in turn depends on the quality of the initial data and might not be available at the very early stages of the analysis. We propose a novel deep-learning approach for improving quality of single particle datasets. The two-stage procedure consists of denoising single particle images using Variational AutoEncoder framework followed by particle quality filtering based on the score inferred for every particle by Domain Adaptation Neural Network trained on a large data set of categorised 2D averages. This approach allows an automated scoring of noisy raw images using data patterns learned from the high signal-to-noise ratio, externally derived 2D classes. Consequently, a higher quality data set enters computationally expensive steps of the data analysis, reducing the need for protracted and expensive calculations. Importantly, our method does not require any prior knowledge about the data or existence of a 3D model, making it universally applicable. Tests on publicly available datasets demonstrated that our approach largely outperformed 2D class-based particle discrimination. Smaller subsets of the top-scoring particles selected with our method were required to obtain the author-reported 3D model resolution. When applied to the user data in the automated on-the-fly data processing pipeline, the method rescued 30% of cases, which otherwise would not reach confidence threshold required for making decision to proceed to the 3D model refinement. It also led to general improvements in the quality of the 3D models for many datasets which were selected for the high-resolution processing.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

Malhotra, S., Hatton, D., Jackson, S., Iadanza, M., Joseph, A. P., Palmer, C., Thiyagalingam, J., Burnley, T., Chaban, Y.. 2025-11-13. Automated filtering of particle images in single particle cryoEM. https://doi.org/10.1101/2025.11.12.688030

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related preprints

Mechanism of molecular recognition revealed through dynamic drug binding pathways to SARS-CoV-2 main protease

Characterization of drug-binding pathways remains experimentally limited by transient intermediates and computationally challenging due to long timescales intractable for conventional molecular dynamics. To address these challenges, we combined solution NMR titrations with weighted ensemble (WE) enhanced sampling simulations to resolve atomistic pathways of nirmatrelvir binding to the SARS-CoV-2 main protease. NMR titration revealed residue-dependent heterogeneity spanning fast, intermediate, and slow exchange regimes. WE simulations complement the NMR by providing insights into unassigned residues and adding time-resolved and three-dimensional structural context. We map key interactions along two distinct binding pathways, provide dynamic explanations for residues involved in resistance, and capture unique backbone conformations compared to those sampled in unbound or bound states. Our comprehensive binding model is consistent with a combined conformational selection and induced fit mechanism in which early transient contacts are made with residues E47 and L50 and allosteric motions are centered around residue V204 of the distal domain. This synergistic application of WE and titration NMR enables a more comprehensive characterization of drug binding than either method alone, providing an integrated framework that may have broader applicability to defining structure-kinetic relationships and guiding design of next-generation inhibitors.

biophysics↗

Fibers and Glasses are Competing Material States in FUS Protein Condensation

Dense, well-ordered material states of proteins form the amyloid fibers that are a hallmark of neurodegenerative disease in the brain. Beyond forming amyloid fibers, some of these proteins can also adopt other material states termed condensates which are initially liquid-like but evolve to a soft, glassy phase. Fiber growth requires a large supply of monomers and, thus, it is often speculated that fibers emerge from within a dense condensate as it ages and its microscopic dynamics slow into a glassy state. Here, we use the well-established model system Fused in Sarcoma (FUS) to directly observe, quantify and theoretically describe fiber growth and its interplay with condensates. We report the discovery that fibers grow overwhelmingly in the dilute phase surrounding the condensates while the condensates concurrently evolve to a glassy arrested solid. The resulting protein fibers and glassy condensates are both distinct solid-like phases that coexist but do not directly interconvert. Taken together, these findings reveal that there are two competitive aging pathways in FUS condensation that are linked through phase separation kinetics.

biophysics↗

A Minimally Perturbative DARPin Probe for Quantitative Fluorescence Imaging of the Human TCR-CD3 Complex

Fluorescence microscopy is a powerful tool for dissecting the molecular mechanisms of T-cell antigen recognition in living cells, but its quantitative insight critically depends on non-perturbative, high-quality probes. Here, we repurpose a small (~15 kDa) CD3epsilon-binding DARPin (designed ankyrin repeat proteins) to a fluorescent label for T-cell receptor (TCR)/CD3 complexes on primary human CD8+ T-cells, with the aim of generating a powerful tool for quantitative analysis, single-molecule tracking, and advanced imaging of TCR dynamics. We show that the DARPin binds CD3{varepsilon} with high affinity and selectivity and using single molecule tracking and brightness analysis, we characterize the TCR-CD3 diffusion behavior and show that the DARPin binds to both CD3epsilon; subunits. Importantly, labeling preserves antigen sensitivity: on supported lipid bilayers presenting cognate pMHC, T-cells remain responsive, assemble synapses, form TCR microclusters, and initiate signaling similar to unlabeled controls. We further demonstrate compatibility with lattice light-sheet microscopy for volumetric imaging of T-cell - APC interactions in living cells. Together, these results establish DARPins as versatile, minimally perturbative probes for high resolution, quantitative studies of T cell synapse organization and signaling.

biophysics↗