ArticleActa crystallographica. Section D, Structural biology2019
Flexible workflows for on-the-fly electron-microscopy single-particle image processing using Scipion.
Article in Acta crystallographica. Section D, Structural biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Current and future perspectives for structural biology at the Grenoble EPN campus: a comprehensive overview.Journal of synchrotron radiation · 2025Review
- TomoTwin: generalized 3D localization of macromolecules in cryo-electron tomograms with structural data mining.Nature methods · 2023Article
- Advances in Xmipp for Cryo-Electron Microscopy: From Xmipp to Scipion.Molecules (Basel, Switzerland) · 2021Article
- SINGLE: Atomic-resolution structure identification of nanocrystals by graphene liquid cell EM.Science advances · 2021Article
- TranSPHIRE: automated and feedback-optimized on-the-fly processing for cryo-EM.Nature communications · 2020Article
- The evolution of SPHIRE-crYOLO particle picking and its application in automated cryo-EM processing workflows.Communications biology · 2020Article
- SIMPLE 3.0. Stream single-particle cryo-EM analysis in real time.Journal of structural biology: X · 2020Article
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Authors and funding
20 authors.
Funding
Abstract
Electron microscopy of macromolecular structures is an approach that is in increasing demand in the field of structural biology. The automation of image acquisition has greatly increased the potential throughput of electron microscopy. Here, the focus is on the possibilities in Scipion to implement flexible and robust image-processing workflows that allow the electron-microscope operator and the user to monitor the quality of image acquisition, assessing very simple acquisition measures or obtaining a first estimate of the initial volume, or the data resolution and heterogeneity, without any need for programming skills. These workflows can implement intelligent automatic decisions and they can warn the user of possible acquisition failures. These concepts are illustrated by analysis of the well known 2.2 Å resolution β-galactosidase data set.
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