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TitleMemBrain v2: an end-to-end tool for the analysis of membranes in cryo-electron tomography.
Journal, issue, pagesNat Methods, Year 2026
Publish dateSep 8, 2026
AuthorsLorenz Lamm / Simon Zufferey / Hanyi Zhang / Ricardo D Righetto / Florent Waltz / Wojciech Wietrzynski / Kevin A Yamauchi / Alister Burt / Ye Liu / Antonio Martinez-Sanchez / Sebastian Ziegler / Fabian Isensee / Julia A Schnabel / Benjamin D Engel / Tingying Peng /
PubMed AbstractCryo-electron tomography provides unique insights into macromolecular complexes in their native environments, yet membrane analysis remains a major bottleneck due to low signal-to-noise ratios, ...Cryo-electron tomography provides unique insights into macromolecular complexes in their native environments, yet membrane analysis remains a major bottleneck due to low signal-to-noise ratios, missing wedge artifacts and the complexity of membrane-associated particles. Existing tools often require extensive manual annotation, struggle with generalization across datasets and lack integrated solutions for segmentation, particle localization and quantitative analysis. We introduce MemBrain v2, a deep-learning-enabled framework that unifies these tasks into a streamlined pipeline. MemBrain-seg leverages a diverse, collaboratively generated training dataset and specialized model training strategies to achieve generalizable membrane segmentation across variable tomographic conditions. MemBrain-pick enables data-efficient localization of membrane-bound particles by integrating geometric constraints with deep learning, reducing the need for extensive manual annotation. MemBrain-stats provides quantitative insights into particle distributions, computing spatial metrics to analyze intramembrane particle organization. MemBrain v2 integrates seamlessly into cryo-electron tomography workflows, providing an accessible and structured approach to membrane analysis.
External linksNat Methods / PubMed:42711494
MethodsEM (subtomogram averaging)
Resolution22.7 Å
Structure data

EMDB-54837: Chlamydomonas nuclear envelope-bound ribosome
Method: EM (subtomogram averaging) / Resolution: 22.7 Å

Source
  • Chlamydomonas reinhardtii (plant)

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