ArticleProtein expression and purification2013
A general path for large-scale solubilization of cellular proteins: from membrane receptors to multiprotein complexes.
Article in Protein expression and purification, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- One-step nanoscale expansion microscopy reveals individual protein shapes.Nature biotechnology · 2025Article
- Structural basis of transcription: RNA polymerase II substrate binding and metal coordination using a free-electron laser.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Membrane proteome of the thermoalkaliphileFrontiers in microbiology · 2023Article
- Optimizing the Expression and Solubilization of an E. coli-Produced Leukemia Inhibitory Factor for Anti-LIF Antibody Production and Use Thereof for Contraception in Mice.Molecular biotechnology · 2021Article
- High-throughput Preparation of DNA, RNA, and Protein from Cryopreserved Human iPSCs for Multi-omics Analysis.Current protocols in stem cell biology · 2020Article
- Transmission electron microscopy for the evaluation and optimization of crystal growth.Acta crystallographica. Section D, Structural biology · 2016Article
- High-density grids for efficient data collection from multiple crystals.Acta crystallographica. Section D, Structural biology · 2016Article
- WNT5A inhibits hepatocyte proliferation and concludes β-catenin signaling in liver regeneration.The American journal of pathology · 2015Article
- Crystal Structure of a Transcribing RNA Polymerase II Complex Reveals a Complete Transcription Bubble.Molecular cell · 2015Article
- Endosomal GPCR signaling turned off by negative feedback actions of PKA and v-ATPase.Nature chemical biology · 2014Article
- Transmission electron microscopy as a tool for nanocrystal characterization pre- and post-injector.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2014Article
- Use of transmission electron microscopy to identify nanocrystals of challenging protein targets.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
Corrections and comments
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Authors and funding
17 authors.
Funding
Abstract
Expression of recombinant proteins in bacterial or eukaryotic systems often results in aggregation rendering them unavailable for biochemical or structural studies. Protein aggregation is a costly problem for biomedical research. It forces research laboratories and the biomedical industry to search for alternative, more soluble, non-human proteins and limits the number of potential "druggable" targets. In this study we present a highly reproducible protocol that introduces the systematic use of an extensive number of detergents to solubilize aggregated proteins expressed in bacterial and eukaryotic systems. We validate the usefulness of this protocol by solubilizing traditionally difficult human protein targets to milligram quantities and confirm their biological activity. We use this method to solubilize monomeric or multimeric components of multi-protein complexes and demonstrate its efficacy to reconstitute large cellular machines. This protocol works equally well on cytosolic, nuclear and membrane proteins and can be easily adapted to a high throughput format.
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