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[Submitted on 15 Oct 2026] Title:Learning the Shared Latent Structure of Cryo-EM Inverse Problems View a PDF of the paper titled Learning the Shared Latent Structure of Cryo-EM Inverse Problems, by Nithin Chalapathi and 6 other authors View PDF HTML (experimental) Abstract:Understanding biomolecular function requires characterizing three-dimensional structure and conformational variability, for which cryogenic electron microscopy (cryo-EM) is a powerful tool. Cryo-EM produces noisy two-dimensional particle images in which molecular structure, particle pose, and imaging conditions are jointly encoded. Recovering biological information from these observations spans inverse problems including pose estimation, heterogeneity analysis, and reconstruction. These tasks are usually addressed independently despite shared protein structure and image formation, motivating a common representation across inverse problems. Since biologically meaningful differences may be spatially localized, we study self-distillation with complementary global and masked patch objectives. Because experimental dataset discrimination can reflect acquisition-specific cues, we develop controlled synthetic and experimental evaluations and find that structural discrimination benefits from dense spatial features. We introduce the EMber family of vision transformers, pre-trained on >50 million experimental particle images from 214 EMPIAR datasets together with simulated projections from 268,000 molecular assemblies. EMber improves upon existing methods at conformational and compositional discrimination by 14.85 and 14.26 percentage points, estimates conformational populations to within 1.59pp error with a linear probe, and produces particle assignments yielding reference-quality reconstructions in fewer epochs. We demonstrate how to learn representations that capture biological information for use across multiple cryo-EM inverse problems. Subjects: Computer Vision and Pattern Recognition (cs.CV); Machine Learning (cs.LG); Quantitative Methods (q-bio.QM) Cite as: arXiv:2610.22523 [cs.CV] (or arXiv:2610.22523v1 [cs.CV] for this version) https://doi.org/10.48550/arXiv.2610.22523 arXiv-issued DOI via DataCite (pending registration) Submission history From: Nithin Chalapathi [view email] [v1] Thu, 15 Oct 2026 18:17:29 UTC (29,010 KB) Full-text links: Access Paper: View a PDF of the paper titled Learning the Shared Latent Structure of Cryo-EM Inverse Problems, by Nithin Chalapathi and 6 other authors View PDF HTML (experimental) TeX Source view license Additional Features Audio Summary Current browse context: cs.CV new | recent | 2026-10 Change to browse by: cs cs.LG q-bio q-bio.QM References & Citations NASA ADS Google Scholar Semantic Scholar Loading... Data provided by: Bibliographic Tools Bibliographic and Citation Tools Bibliographic Explorer Toggle Bibliographic Explorer (What is the Explorer?) Connected Papers Toggle Connected Papers (What is Connected Papers?) Litmaps Toggle Litmaps (What is Litmaps?) scite.ai Toggle scite Smart Citations (What are Smart Citations?) Code, Data, Media Code, Data and Media Associated with this Article alphaXiv Toggle alphaXiv (What is alphaXiv?) Links to Code Toggle CatalyzeX Code Finder for Papers (What is CatalyzeX?) DagsHub Toggle DagsHub (What is DagsHub?) GotitPub Toggle Gotit.pub (What is GotitPub?) Huggingface Toggle Hugging Face (What is Huggingface?) ScienceCast Toggle ScienceCast (What is ScienceCast?) Demos Demos Replicate Toggle Replicate (What is Replicate?) Spaces Toggle Hugging Face Spaces (What is Spaces?) Spaces Toggle TXYZ.AI (What is TXYZ.AI?) Related Papers Recommenders and Search Tools Link to Influence Flower Influence Flower (What are Influence Flowers?) Core recommender toggle CORE Recommender (What is CORE?) Author Venue Institution Topic About arXivLabs arXivLabs: experimental projects with community collaborators arXivLabs is a framework that allows collaborators to develop and share new arXiv features directly on our website. Both individuals and organizations that work with arXivLabs have embraced and accepted our values of openness, community, excellence, and user data privacy. arXiv is committed to these values and only works with partners that adhere to them. Have an idea for a project that will add value for arXiv's community? Learn more about arXivLabs. Which authors of this paper are endorsers? | Disable MathJax (What is MathJax?)