ArticleScientific reports2017
X-ray diffraction reveals the intrinsic difference in the physical properties of membrane and soluble proteins.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 22 citations in OpenAlex.
- X-ray diffraction images for two membrane protein crystals presenting high anisotropy; theIUCrData · 2025Article
- Article
- CryoEM Data Analysis of Membrane Proteins. Practical Considerations on Amphipathic Belts, Ligands, and Variability Analysis.Methods in molecular biology (Clifton, N.J.) · 2024Review
- Diffraction anisotropy and paired refinement: crystal structure of H33, a protein binder to interleukin 10.Journal of applied crystallography · 2023Article
- A comparative anatomy of protein crystals: lessons from the automatic processing of 56 000 samples.IUCrJ · 2019Article
- Structure of an engineered multidrug transporter MdfA reveals the molecular basis for substrate recognition.Communications biology · 2019Article
- Article
- Quantitative comparison of ABC membrane protein type I exporter structures in a standardized way.Computational and structural biotechnology journal · 2018Article
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Authors and funding
9 authors at 3 institutions in 3 countries.
Funding
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Abstract
Membrane proteins are distinguished from soluble proteins by their insertion into biological membranes. This insertion is achieved via a noticeable arrangement of hydrophobic amino acids that are exposed at the surface of the protein, and renders the interaction with the aliphatic tails of lipids more energetically favorable. This important difference between these two categories of proteins is the source of the need for a specific handling of membrane proteins, which transpired in the creation of new tools for their recombinant expression, purification and even crystallization. Following this line, we show here that crystals of membrane proteins display systematically higher diffraction anisotropy than those of soluble proteins. This phenomenon dramatically hampers structure solution and refinement, and has a strong impact on the quality of electron-density maps. A farther search for origins of this phenomenon showed that the type of crystallization, and thus the crystal packing, has no impact on anisotropy, nor does the nature or function of the membrane protein. Membrane proteins fully embedded within the membrane display equal anisotropy compared to the ones with extra membranous domains or fusions with soluble proteins. Overall, these results overturn common beliefs and call for a specific handling of their diffraction data.
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