ArticleCommunications biology2024
An immobilized antibody-based affinity grid strategy for on-grid purification of target proteins enables high-resolution cryo-EM.
Article in Communications biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- In vitro, cellular and in vivo studies of amyloid oligomers structure and toxicity: Challenges and advances.Protein science : a publication of the Protein Society · 2026Review
- Advances in Crystallography and Cryo-Electron Microscopy for the Study of Membrane Proteins.Advances in experimental medicine and biology · 2026Review
- Identification of key amino acids defining conformational neutralizing epitopes of coxsackievirus A5 using monoclonal antibody escape mutants.Frontiers in immunology · 2026Article
- Nickel-NTA lipid-monolayer affinity grids allow for high-resolution structure determination by cryo-EM.Journal of structural biology · 2025Article
- Overcoming Preferred Orientation in Cryo-EM With Ultrasonic Excitation During Vitrification.bioRxiv : the preprint server for biology · 2025Article
- CryoEM grid preparation: a closer look at advancements and impact of preparation mode and new approaches.Biochemical Society transactions · 2024Review
Corrections and comments
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Authors and funding
12 authors.
Funding
Abstract
In cryo-electron microscopy (cryo-EM), sample preparation poses a critical bottleneck, particularly for rare or fragile macromolecular assemblies and those suffering from denaturation and particle orientation distribution issues related to air-water interface. In this study, we develop and characterize an immobilized antibody-based affinity grid (IAAG) strategy based on the high-affinity PA tag/NZ-1 antibody epitope tag system. We employ Pyr-NHS as a linker to immobilize NZ-1 Fab on the graphene oxide or carbon-covered grid surface. Our results demonstrate that the IAAG grid effectively enriches PA-tagged target proteins and overcomes preferred orientation issues. Furthermore, we demonstrate the utility of our IAAG strategy for on-grid purification of low-abundance target complexes from cell lysates, enabling atomic resolution cryo-EM. This approach greatly streamlines the purification process, reduces the need for large quantities of biological samples, and addresses common challenges encountered in cryo-EM sample preparation. Collectively, our IAAG strategy provides an efficient and robust means for combined sample purification and vitrification, feasible for high-resolution cryo-EM. This approach holds potential for broader applicability in both cryo-EM and cryo-electron tomography (cryo-ET).
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Registered trials
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