ArticleIUCrJ2020
The resolution revolution in cryoEM requires high-quality sample preparation: a rapid pipeline to a high-resolution map of yeast fatty acid synthase.
Article in IUCrJ, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 26 citations in OpenAlex.
- Structural basis of product recognition by Mycobacterium tuberculosis fatty acid synthase.Protein science : a publication of the Protein Society · 2026Article
- CryoDRGN-ET: deep reconstructing generative networks for visualizing dynamic biomolecules inside cells.Nature methods · 2024Article
- VitroJet: new features and case studies.Acta crystallographica. Section D, Structural biology · 2024Article
- Direct structural analysis of a single acyl carrier protein domain in fatty acid synthase from the fungus Saccharomyces cerevisiae.Communications biology · 2024Article
- Article
- Developing Graphene Grids for Cryoelectron Microscopy.Frontiers in molecular biosciences · 2022Review
- Fatty Acid Synthase: Structure, Function, and Regulation.Sub-cellular biochemistry · 2022Review
- Elusive structure of mammalian DGKs.Advances in biological regulation · 2022Review
- Perspective: Biochemical and Physical Constraints Associated With Preparing Thin Specimens for Single-Particle Cryo-EM.Frontiers in molecular biosciences · 2022Article
- Biophysical Screening Pipeline for Cryo-EM Grid Preparation of Membrane Proteins.Frontiers in molecular biosciences · 2022Article
- Application of Monolayer Graphene and Its Derivative in Cryo-EM Sample Preparation.International journal of molecular sciences · 2021Review
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Single-particle electron cryo-microscopy (cryoEM) has undergone a 'resolution revolution' that makes it possible to characterize megadalton (MDa) complexes at atomic resolution without crystals. To fully exploit the new opportunities in molecular microscopy, new procedures for the cloning, expression and purification of macromolecular complexes need to be explored. Macromolecular assemblies are often unstable, and invasive construct design or inadequate purification conditions and sample-preparation methods can result in disassembly or denaturation. The structure of the 2.6 MDa yeast fatty acid synthase (FAS) has been studied by electron microscopy since the 1960s. Here, a new, streamlined protocol for the rapid production of purified yeast FAS for structure determination by high-resolution cryoEM is reported. Together with a companion protocol for preparing cryoEM specimens on a hydrophilized graphene layer, the new protocol yielded a 3.1 Å resolution map of yeast FAS from 15 000 automatically picked particles within a day. The high map quality enabled a complete atomic model of an intact fungal FAS to be built.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.