bioRxiv Science⌕ Search

Biology subjects

Ramirez-Aportela, E.

Publications and source records attributed to Ramirez-Aportela, E..

3 recordsLinked to original sources

AlignPCA-2D: PCA-Reduced Euclidean Vector Alignment for 2D Classification in Cryo-EM

Cryogenic Electron Microscopy (cryo-EM) has transformed structural biology by enabling high-resolution reconstruction of macromolecular complexes from noisy projection images. However, the intrinsic heterogeneity and low signal-to-noise ratio of cryo-EM datasets make 2D classification a critical and computationally demanding step in the processing work-flow. Here, we introduce AlignPCA-2D, a PCA-space Euclidean vector alignment method for fast, interpretable 2D classification in cryo-EM. By projecting particle images and class representations into a compressed latent PCA space, AlignPCA-2D reduces data dimensionality while pre-serving meaningful structural variability. The image-to-class assignment is then performed using Euclidean distance, enabling efficient and accurate classification. We benchmark AlignPCA-2D against established cryo-EM software, such as RELION and cryoSPARC, and demonstrate that it achieves competitive alignment accuracy while substantially reducing computational cost. This approach provides a lightweight alternative for large-scale 2D classification tasks, and its modular design makes it compatible with existing cryo-EM processing pipelines. O_TBL View this table: org.highwire.dtl.DTLVardef@1e384org.highwire.dtl.DTLVardef@2474org.highwire.dtl.DTLVardef@15966c1org.highwire.dtl.DTLVardef@6934adorg.highwire.dtl.DTLVardef@1017b4e_HPS_FORMAT_FIGEXP M_TBL O_FLOATNOTable 2.C_FLOATNO O_TABLECAPTIONParticle retention and overlap among 2D classification methods C_TABLECAPTION C_TBL

biophysics↗

FSC-Q: A CryoEM map-to-atomic model quality validation based on the local Fourier Shell Correlation

In recent years, advances in cryoEM have dramatically increased the resolution of Coulomb potential maps and, with it, the number of solved atomic models. It is widely accepted that the quality of cryoEM maps varies locally; therefore, the evaluation of the maps-derived structural models must be done locally as well. In this article, a method for the local analysis of the map-to-model fit is presented. The algorithm uses a comparison of two local resolution maps. The first is the local FSC (Fourier shell correlation) between the full map and the model, while the second is calculated between the half maps normally used in typical single particle analysis workflows. We call the new quality measure "FSC-Q", and it is a quantitative estimation of how much of the model is supported by the signal content of the map. Furthermore, we show that FSC-Q may be helpful to avoid overfitting. It can be used to complement other methods, such as the Q-score method that estimates the resolvability of atoms.

biophysics↗

Automatic local resolution-based sharpening of cryo-EM maps.

Recent technological advances and computational developments, have allowed the reconstruction of cryo-EM maps at near-atomic resolution structures. Cryo-EM maps benefit significantly of a \"postprocessing\" step, normally referred to as \"sharpening\", that tends to increase signal at medium/high resolution. Here, we propose a new method for local sharpening of volumes generated by cryo-EM. The algorithm (LocalDeblur) is based on a local resolution-guided Wiener restoration approach, does not need any prior atomic model and it avoids artificial structure 1 factor corrections. LocalDeblur is fully automatic and parameter free. We show that the new method significantly and quantitatively improving map quality and interpretability, especially in cases of broad local resolution changes (as is often the case of membrane proteins).

biophysics↗