ArticleProtein science : a publication of the Protein Society2007
A high-throughput method for membrane protein solubility screening: the ultracentrifugation dispersity sedimentation assay.
Article in Protein science : a publication of the Protein Society, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 24 papers.
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24 citing papers in PubMed, 62 citations in OpenAlex.
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- ATR-FTIR spectroscopy and spectroscopic imaging to investigate the behaviour of proteins subjected to freeze-thaw cycles in droplets, wells, and under flow.The Analyst · 2021Article
- Membrane Protein Structure Determination and Characterisation by Solution and Solid-State NMR.Biology · 2020Review
- ATR-FTIR spectroscopy and spectroscopic imaging for the analysis of biopharmaceuticals.Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy · 2020Review
- Isolation and Characterization of Nanobodies against a Zinc-Transporting P-Type ATPase.Antibodies (Basel, Switzerland) · 2018Article
- Using a SMALP platform to determine a sub-nm single particle cryo-EM membrane protein structure.Biochimica et biophysica acta. Biomembranes · 2018Article
- In Situ Reconstitution of the Adenosine AJournal of the American Chemical Society · 2017Article
- How Do Short Chain Nonionic Detergents Destabilize G-Protein-Coupled Receptors?Journal of the American Chemical Society · 2016Article
- Direct evidence of the molecular basis for biological silicon transport.Nature communications · 2016Article
- Membrane proteins: always an insoluble problem?Biochemical Society transactions · 2016Review
- The Effect of Detergent, Temperature, and Lipid on the Oligomeric State of MscL Constructs: Insights from Mass Spectrometry.Chemistry & biology · 2015Article
- The use of SMALPs as a novel membrane protein scaffold for structure study by negative stain electron microscopy.Biochimica et biophysica acta · 2015Article
- High-throughput thermal stability analysis of a monoclonal antibody by attenuated total reflection FT-IR spectroscopic imaging.Analytical chemistry · 2014Article
- A structural biology approach to understand human lymphatic filarial infection.PLoS neglected tropical diseases · 2014Article
- Solubilization and stabilization of isolated photosystem I complex with lipopeptide detergents.PloS one · 2013Article
- Article
- Engineering an ultra-thermostable β(1)-adrenoceptor.Journal of molecular biology · 2011Article
- A high-throughput differential filtration assay to screen and select detergents for membrane proteins.Analytical biochemistry · 2010Article
- Effective critical micellar concentration of a zwitterionic detergent: a fluorimetric study on n-dodecyl phosphocholine.Journal of fluorescence · 2010Article
Corrections and comments
- Erratum issuedPostis, Vincent [added]; Xia, Xiaobing [added]
Authors and funding
9 authors at 3 institutions in 1 country.
Funding
Abstract
One key to successful crystallization of membrane proteins is the identification of detergents that maintain the protein in a soluble, monodispersed state. Because of their hydrophobic nature, membrane proteins are particularly prone to forming insoluble aggregates over time. This nonspecific aggregation of the molecules reduces the likelihood of the regular association of the protein molecules essential for crystal lattice formation. Critical buffer components affecting the aggregation of membrane proteins include detergent choice, salt concentration, and presence of glycerol. The optimization of these parameters is often a time- and protein-consuming process. Here we describe a novel ultracentrifugation dispersity sedimentation (UDS) assay in which ultracentrifugation of very small (5 microL) volumes of purified, soluble membrane protein is combined with SDS-PAGE analysis to rapidly assess the degree of protein aggregation. The results from the UDS method correlate very well with established methods like size-exclusion chromatography (SEC), while consuming considerably less protein. In addition, the UDS method allows rapid screening of detergents for membrane protein crystallization in a fraction of the time required by SEC. Here we use the UDS method in the identification of suitable detergents and buffer compositions for the crystallization of three recombinant prokaryotic membrane proteins. The implications of our results for membrane protein crystallization prescreening are discussed.
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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.