Pavol Harar, Lukas Herrmann, Philipp Grohs, David Haselbach
{"title":"FakET: Simulating cryo-electron tomograms with neural style transfer","authors":"Pavol Harar, Lukas Herrmann, Philipp Grohs, David Haselbach","doi":"10.1016/j.str.2025.01.020","DOIUrl":null,"url":null,"abstract":"In cryo-electron microscopy, accurate particle localization and classification are imperative. Recent deep learning solutions, though successful, require extensive training datasets. The protracted generation time of physics-based models, often employed to produce these datasets, limits their broad applicability. We introduce FakET, a method based on neural style transfer, capable of simulating the forward operator of any cryo transmission electron microscope. It can be used to adapt a synthetic training dataset according to reference data producing high-quality simulated micrographs or tilt-series. To assess the quality of our generated data, we used it to train a state-of-the-art localization and classification architecture and compared its performance with a counterpart trained on benchmark data. Remarkably, our technique matches the performance, boosts data generation speed <span><span style=\"\"></span><span data-mathml='<math xmlns=\"http://www.w3.org/1998/Math/MathML\"><mrow is=\"true\"><mn is=\"true\">750</mn><mo linebreak=\"goodbreak\" linebreakstyle=\"after\" is=\"true\">&#xD7;</mo></mrow></math>' role=\"presentation\" style=\"font-size: 90%; display: inline-block; position: relative;\" tabindex=\"0\"><svg aria-hidden=\"true\" focusable=\"false\" height=\"1.971ex\" role=\"img\" style=\"vertical-align: -0.235ex;\" viewbox=\"0 -747.2 2280 848.5\" width=\"5.296ex\" xmlns:xlink=\"http://www.w3.org/1999/xlink\"><g fill=\"currentColor\" stroke=\"currentColor\" stroke-width=\"0\" transform=\"matrix(1 0 0 -1 0 0)\"><g is=\"true\"><g is=\"true\"><use xlink:href=\"#MJMAIN-37\"></use><use x=\"500\" xlink:href=\"#MJMAIN-35\" y=\"0\"></use><use x=\"1001\" xlink:href=\"#MJMAIN-30\" y=\"0\"></use></g><g is=\"true\" transform=\"translate(1501,0)\"><use xlink:href=\"#MJMAIN-D7\"></use></g></g></g></svg><span role=\"presentation\"><math xmlns=\"http://www.w3.org/1998/Math/MathML\"><mrow is=\"true\"><mn is=\"true\">750</mn><mo is=\"true\" linebreak=\"goodbreak\" linebreakstyle=\"after\">×</mo></mrow></math></span></span><script type=\"math/mml\"><math><mrow is=\"true\"><mn is=\"true\">750</mn><mo linebreak=\"goodbreak\" linebreakstyle=\"after\" is=\"true\">×</mo></mrow></math></script></span>, uses <span><span style=\"\"></span><span data-mathml='<math xmlns=\"http://www.w3.org/1998/Math/MathML\"><mrow is=\"true\"><mn is=\"true\">33</mn><mo linebreak=\"goodbreak\" linebreakstyle=\"after\" is=\"true\">&#xD7;</mo></mrow></math>' role=\"presentation\" style=\"font-size: 90%; display: inline-block; position: relative;\" tabindex=\"0\"><svg aria-hidden=\"true\" focusable=\"false\" height=\"1.971ex\" role=\"img\" style=\"vertical-align: -0.235ex;\" viewbox=\"0 -747.2 1779.5 848.5\" width=\"4.133ex\" xmlns:xlink=\"http://www.w3.org/1999/xlink\"><g fill=\"currentColor\" stroke=\"currentColor\" stroke-width=\"0\" transform=\"matrix(1 0 0 -1 0 0)\"><g is=\"true\"><g is=\"true\"><use xlink:href=\"#MJMAIN-33\"></use><use x=\"500\" xlink:href=\"#MJMAIN-33\" y=\"0\"></use></g><g is=\"true\" transform=\"translate(1001,0)\"><use xlink:href=\"#MJMAIN-D7\"></use></g></g></g></svg><span role=\"presentation\"><math xmlns=\"http://www.w3.org/1998/Math/MathML\"><mrow is=\"true\"><mn is=\"true\">33</mn><mo is=\"true\" linebreak=\"goodbreak\" linebreakstyle=\"after\">×</mo></mrow></math></span></span><script type=\"math/mml\"><math><mrow is=\"true\"><mn is=\"true\">33</mn><mo linebreak=\"goodbreak\" linebreakstyle=\"after\" is=\"true\">×</mo></mrow></math></script></span> less memory, and scales well to typical transmission electron microscope detector sizes. It leverages GPU acceleration and parallel processing. The source code is available at <span><span>https://github.com/paloha/faket/</span><svg aria-label=\"Opens in new window\" focusable=\"false\" height=\"20\" viewbox=\"0 0 8 8\"><path d=\"M1.12949 2.1072V1H7V6.85795H5.89111V2.90281L0.784057 8L0 7.21635L5.11902 2.1072H1.12949Z\"></path></svg></span>.","PeriodicalId":22168,"journal":{"name":"Structure","volume":"129 1","pages":""},"PeriodicalIF":4.4000,"publicationDate":"2025-02-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Structure","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.1016/j.str.2025.01.020","RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
引用次数: 0
Abstract
In cryo-electron microscopy, accurate particle localization and classification are imperative. Recent deep learning solutions, though successful, require extensive training datasets. The protracted generation time of physics-based models, often employed to produce these datasets, limits their broad applicability. We introduce FakET, a method based on neural style transfer, capable of simulating the forward operator of any cryo transmission electron microscope. It can be used to adapt a synthetic training dataset according to reference data producing high-quality simulated micrographs or tilt-series. To assess the quality of our generated data, we used it to train a state-of-the-art localization and classification architecture and compared its performance with a counterpart trained on benchmark data. Remarkably, our technique matches the performance, boosts data generation speed , uses less memory, and scales well to typical transmission electron microscope detector sizes. It leverages GPU acceleration and parallel processing. The source code is available at https://github.com/paloha/faket/.
期刊介绍:
Structure aims to publish papers of exceptional interest in the field of structural biology. The journal strives to be essential reading for structural biologists, as well as biologists and biochemists that are interested in macromolecular structure and function. Structure strongly encourages the submission of manuscripts that present structural and molecular insights into biological function and mechanism. Other reports that address fundamental questions in structural biology, such as structure-based examinations of protein evolution, folding, and/or design, will also be considered. We will consider the application of any method, experimental or computational, at high or low resolution, to conduct structural investigations, as long as the method is appropriate for the biological, functional, and mechanistic question(s) being addressed. Likewise, reports describing single-molecule analysis of biological mechanisms are welcome.
In general, the editors encourage submission of experimental structural studies that are enriched by an analysis of structure-activity relationships and will not consider studies that solely report structural information unless the structure or analysis is of exceptional and broad interest. Studies reporting only homology models, de novo models, or molecular dynamics simulations are also discouraged unless the models are informed by or validated by novel experimental data; rationalization of a large body of existing experimental evidence and making testable predictions based on a model or simulation is often not considered sufficient.