ArticleActa crystallographica. Section F, Structural biology communications2015
Systematic analysis of protein-detergent complexes applying dynamic light scattering to optimize solutions for crystallization trials.
Article in Acta crystallographica. Section F, Structural biology communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Raynals, an online tool for the analysis of dynamic light scattering.Acta crystallographica. Section D, Structural biology · 2023Article
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- InvasiveFrontiers in cellular and infection microbiology · 2023Article
- Oligomeric state of the aspartate:alanine transporter from Tetragenococcus halophilus.Journal of biochemistry · 2022Article
- Shelterin is a dimeric complex with extensive structural heterogeneity.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Cryo-EM structure of the human CST-Polα/primase complex in a recruitment state.Nature structural & molecular biology · 2022Article
- Measuring Protein Aggregation and Stability Using High-Throughput Biophysical Approaches.Frontiers in molecular biosciences · 2022Article
- Pre-termination Transcription Complex: Structure and Function.Molecular cell · 2021Article
- Selection of Biophysical Methods for Characterisation of Membrane Proteins.International journal of molecular sciences · 2019Review
- Ligand-Induced Coupling between Oligomers of the MBiophysical journal · 2018Article
- Pseudomonas stutzeri as an alternative host for membrane proteins.Microbial cell factories · 2017Article
- Recent applications of light scattering measurement in the biological and biopharmaceutical sciences.Analytical biochemistry · 2016Review
- Use of dynamic light scattering and small-angle X-ray scattering to characterize new surfactants in solution conditions for membrane-protein crystallization.Acta crystallographica. Section F, Structural biology communications · 2015Article
- Stabilization of G protein-coupled receptors by point mutations.Frontiers in pharmacology · 2015Review
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6 authors.
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Abstract
Detergents are widely used for the isolation and solubilization of membrane proteins to support crystallization and structure determination. Detergents are amphiphilic molecules that form micelles once the characteristic critical micelle concentration (CMC) is achieved and can solubilize membrane proteins by the formation of micelles around them. The results are presented of a study of micelle formation observed by in situ dynamic light-scattering (DLS) analyses performed on selected detergent solutions using a newly designed advanced hardware device. DLS was initially applied in situ to detergent samples with a total volume of approximately 2 µl. When measured with DLS, pure detergents show a monodisperse radial distribution in water at concentrations exceeding the CMC. A series of all-trans n-alkyl-β-D-maltopyranosides, from n-hexyl to n-tetradecyl, were used in the investigations. The results obtained verify that the application of DLS in situ is capable of distinguishing differences in the hydrodynamic radii of micelles formed by detergents differing in length by only a single CH2 group in their aliphatic tails. Subsequently, DLS was applied to investigate the distribution of hydrodynamic radii of membrane proteins and selected water-insoluble proteins in presence of detergent micelles. The results confirm that stable protein-detergent complexes were prepared for (i) bacteriorhodopsin and (ii) FetA in complex with a ligand as examples of transmembrane proteins. A fusion of maltose-binding protein and the Duck hepatitis B virus X protein was added to this investigation as an example of a non-membrane-associated protein with low water solubility. The increased solubility of this protein in the presence of detergent could be monitored, as well as the progress of proteolytic cleavage to separate the fusion partners. This study demonstrates the potential of in situ DLS to optimize solutions of protein-detergent complexes for crystallization applications.
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