Skip to content
DraconiticResearch
Search Sources API
190,332 studies31 sourcesUpdated 42 min ago
PreprintCC BYbioRxiv

A learning-to-rank framework for large-scale identification of unknown proteins from cryo-EM and cryo-ET maps

  1. 1Department of Biochemistry and Molecular Biology, Mayo Clinic, Rochester, MN, USA
  2. 2Structural Biology Core, Mayo Clinic, Rochester, MN, USA

Abstract

Cryo-electron microscopy (cryo-EM) and cryo-electron tomography (cryo-ET) can yield density maps whose molecular identities are unknown. Predicted-structure databases enable proteome-scale searches, but distinguishing the correct candidates remains challenging, particularly for intermediate-resolution maps without clear side-chain features. We developed CryoAssign, an automated framework that combines large-scale structure matching with learning-to-rank prioritization. CryoAssign searches intact density maps without prior segmentation and integrates complementary measures of map-model agreement. On held-out benchmark maps, CryoAssign robustly prioritized the correct candidates. It also identified proteins or narrowed the set of candidates in previously unassigned cryo-EM maps and recovered multiple components from complex cryo-EM and cryo-ET maps. Controlled low-pass filtering showed generally robust recovery across a broad range of intermediate resolutions. CryoAssign provides a scalable approach for identifying proteins from cryo-EM and cryo-ET density maps.

Related

  1. VAEBAC: a representation-learning framework for proteome-scale prediction of amyloidogenic proteins and functional stratification of nucleic-acid-binding proteins.
    Muhammad Uzair Ashraf, Owais Ahmad, Rizwan Hasan Khan
    Bioinformatics (Oxford, England)Peer-reviewedCC BYFull textMolecular biology & gene regulationEurope PMCCrossref
  2. Prediction of Residue-Level Base Preference for DNA-Binding Proteins Using a Multimodal Learning Framework
    Siyuan Li, Wenyan He, Mengru Zhang +7
    JACS AuPeer-reviewedCC BY-NC-ND 4.0Full textMolecular biology & gene regulationCrossrefEurope PMCPMC
  3. Large Language Model Framework for Structured Biomarker Extraction and Triple-Negative Breast Cancer Identification From Pathology Reports: Development and Evaluation Study.
    Nirmit Jain, Trisha Annambhotla, Akshara Siddharthan +7
    JMIR formative researchPeer-reviewedCC BYFull textMolecular biology & gene regulationEurope PMC
  4. Identification and characterization of two transmembrane proteins required for virulence of Ustilago maydis
    Paul Weiland, Florian Altegoer
    Frontiers in Plant SciencesPreprintLicence not statedStructural biologyGeneral biologyHAL
  5. FAMUS: a few-shot learning framework for large-scale protein annotation
    Guy Shur, David Burstein
    BioinformaticsPeer-reviewedCC BY 4.0Full textMolecular biology & gene regulationCrossrefPMC
BibTeX
@misc{hu2026learningtorank,
  title = {{A learning-to-rank framework for large-scale identification of unknown proteins from cryo-EM and cryo-ET maps}},
  author = {Qi Hu and Georges Mer},
  howpublished = {bioRxiv},
  year = {2026},
  month = oct,
  doi = {10.64898/2026.10.12.758677},
  url = {https://www.biorxiv.org/content/10.64898/2026.10.12.758677v1},
  note = {CC BY},
}
RIS
TY  - UNPB
TI  - A learning-to-rank framework for large-scale identification of unknown proteins from cryo-EM and cryo-ET maps
AU  - Qi Hu
AU  - Georges Mer
PY  - 2026
DA  - 2026/10/12
PB  - bioRxiv
DO  - 10.64898/2026.10.12.758677
UR  - https://www.biorxiv.org/content/10.64898/2026.10.12.758677v1
AB  - Cryo-electron microscopy (cryo-EM) and cryo-electron tomography (cryo-ET) can yield density maps whose molecular identities are unknown. Predicted-structure databases enable proteome-scale searches, but distinguishing the correct candidates remains challenging, particularly for intermediate-resolution maps without clear side-chain features. We developed CryoAssign, an automated framework that combines large-scale structure matching with learning-to-rank prioritization. CryoAssign searches intact density maps without prior segmentation and integrates complementary measures of map-model agreement. On held-out benchmark maps, CryoAssign robustly prioritized the correct candidates. It also identified proteins or narrowed the set of candidates in previously unassigned cryo-EM maps and recovered multiple components from complex cryo-EM and cryo-ET maps. Controlled low-pass filtering showed generally robust recovery across a broad range of intermediate resolutions. CryoAssign provides a scalable approach for identifying proteins from cryo-EM and cryo-ET density maps.
SN  - 2692-8205
ER  -