ArticleJournal of structural biology2019
3.1 Å structure of yeast RNA polymerase II elongation complex stalled at a cyclobutane pyrimidine dimer lesion solved using streptavidin affinity grids.
Article in Journal of structural biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- Overcoming air-water interface-induced artifacts in cryo-EM with protein nanocrates.Nature methods · 2026Article
- Sub-2 Å cryo-EM structures of transcribing RNA polymerase II reveal critical roles of water molecules in catalysis.Molecular cell · 2026Article
- Mechanisms of transcription-coupled repair and DNA damage surveillance in health and disease.Nature reviews. Molecular cell biology · 2026Review
- Overcoming air-water interface-induced artifacts in Cryo-EM with protein nanocrates.Research square · 2025Article
- Foam film vitrification for cryo-EM.Nature communications · 2025Article
- Open architecture of archaea MCM and dsDNA complexes resolved using monodispersed streptavidin affinity CryoEM.Nature communications · 2024Article
- An immobilized antibody-based affinity grid strategy for on-grid purification of target proteins enables high-resolution cryo-EM.Communications biology · 2024Article
- Elf1 promotes Rad26's interaction with lesion-arrested Pol II for transcription-coupled repair.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Streptavidin-Affinity Grid Fabrication for Cryo-Electron Microscopy Sample Preparation.Journal of visualized experiments : JoVE · 2023Article
- A direct interaction between CPF and RNA Pol II links RNA 3' end processing to transcription.Molecular cell · 2023Article
- Lis1 relieves cytoplasmic dynein-1 autoinhibition by acting as a molecular wedge.Nature structural & molecular biology · 2023Article
- A 3D-printed flow-cell for on-grid purification of electron microscopy samples directly from lysate.Journal of structural biology · 2023Article
- Formation of thyroid hormone revealed by a cryo-EM structure of native bovine thyroglobulin.Nature communications · 2022Article
- RNA polymerase pausing, stalling and bypass during transcription of damaged DNA: from molecular basis to functional consequences.Nucleic acids research · 2022Review
- Article
- Perspective: Biochemical and Physical Constraints Associated With Preparing Thin Specimens for Single-Particle Cryo-EM.Frontiers in molecular biosciences · 2022Article
- Developing Graphene Grids for Cryoelectron Microscopy.Frontiers in molecular biosciences · 2022Review
- A cryo-electron microscopy support film formed by 2D crystals of hydrophobin HFBI.Nature communications · 2021Article
- Mechanism of Rad26-assisted rescue of stalled RNA polymerase II in transcription-coupled repair.Nature communications · 2021Article
- Cryo-electron Microscopy Structure, Assembly, and Mechanics Show Morphogenesis and Evolution of Human Picobirnavirus.Journal of virology · 2020Article
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7 authors.
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Abstract
Despite significant advances in all aspects of single particle cryo-electron microscopy (cryo-EM), specimen preparation still remains a challenge. During sample preparation, macromolecules interact with the air-water interface, which often leads to detrimental effects such as denaturation or adoption of preferred orientations, ultimately hindering structure determination. Randomly biotinylating the protein of interest (for example, at its primary amines) and then tethering it to a cryo-EM grid coated with two-dimensional crystals of streptavidin (acting as an affinity surface) can prevent the protein from interacting with the air-water interface. Recently, this approach was successfully used to solve a high-resolution structure of a test sample, a bacterial ribosome. However, whether this method can be used for samples where interaction with the air-water interface has been shown to be problematic remains to be determined. Here we report a 3.1 Å structure of an RNA polymerase II elongation complex stalled at a cyclobutane pyrimidine dimer lesion (Pol II EC(CPD)) solved using streptavidin grids. Our previous attempt to solve this structure using conventional sample preparation methods resulted in a poor quality cryo-EM map due to Pol II EC(CPD)'s adopting a strong preferred orientation. Imaging the same sample on streptavidin grids improved the angular distribution of its view, resulting in a high-resolution structure. This work shows that streptavidin affinity grids can be used to address known challenges posed by the interaction with the air-water interface.
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