Journal of Structural BiologyBiophysicsPeer-reviewed journal article
Preserving Information and Integrity in Cryo-EM: A Fourier-Space Deposition Approach
Zbyszek OtwinowskiiD, Yirui GuoiD, Raquel BrombergiD, Dominika BorekiD
Abstract
Current guidelines for depositing cryogenic electron microscopy single particle reconstruction (cryo-EM SPR) data require submission of unfiltered, unmasked, and unsharpened raw half-maps. The Fourier Shell Correlation (FSC) between the half-maps is then used as a proxy for the signal-to-noise ratio (SNR) to estimate the reconstructions resolution. This policy was introduced to enable independent validation of reported resolutions. Although developed to safeguard data integrity and minimize bias, these guidelines do not account for specific features of modern cryo-EM processing software, in particular weighting schemes that are not retained in half-map depositions and yet in general are necessary to recapitulate resolution estimates. As a results, resolution estimates and other validation statistics based on half-maps FSC may be under- or overestimated. Here, we describe the limitations of the current deposition guidelines and propose an alternative: depositing cryo-EM results in Fourier (reciprocal) space together with the mandatory deposit of molecular masks or their descriptors. This approach addresses the current limitations, preserves critical information from the reconstruction process, and better supports downstream analyses. HighlightsO_LIReciprocal-space deposition to preserve signal and uncertainty estimates. C_LIO_LIMandatory molecular masks deposition for accurate and unbiased FSC validation. C_LIO_LILimitations of half-map-based Fourier Shell Coefficients. C_LIO_LIThe difference maps can be calculated. C_LI Graphical abstract O_FIG O_LINKSMALLFIG WIDTH=200 HEIGHT=137 SRC="FIGDIR/small/690836v1_ufig1.gif" ALT="Figure 1"> View larger version (36K): org.highwire.dtl.DTLVardef@1a35884org.highwire.dtl.DTLVardef@1086af4org.highwire.dtl.DTLVardef@1a5f118org.highwire.dtl.DTLVardef@177815a_HPS_FORMAT_FIGEXP M_FIG C_FIG
- assay: cryo-EM
- research focus: protein structure prediction
- research focus: benchmarking
- approach: deep learning
- approach: statistical model
- Citations
- 0
- FWCI
- 0.00
- Field percentile
- 0th percentile
Reproducibility ledger
Nobody has reported trying to reproduce this paper yet. Did you replicate an experiment or run the code? Your report saves the next lab a week.
Sign in to file a reproducibility report.
Related papers
- Adaptive FDR thresholding of Fourier shell correlation for resolution estimation of cryo-EM maps
M. Beckers, C. Sachse·bioRxiv·Mar 13, 2020
- Robust quality assessment of cryo-EM maps, tomograms and micrographs by statistics-based local resolution estimation
David Kartte, Carsten Sachse·bioRxiv·Feb 5, 2026
- Non-Uniformity of Projection Distributions Attenuates Resolution in Cryo-EM
P. Baldwin, D. Lyumkis·bioRxiv·May 16, 2019
- REASSESSING THE REVOLUTIONS RESOLUTIONS
Marin van Heel, Michael Schatz·bioRxiv·Nov 24, 2017
- Tools for Visualizing and Analyzing Fourier Space Sampling in Cryo-EM
D. Lyumkis, P. R. Baldwin·bioRxiv·Jun 8, 2020
- Self Fourier shell correlation: properties and application to cryo-ET
E. J. Verbeke, M. A. T. Gilles, … A. Singer·bioRxiv·Nov 7, 2023