ArticleBiophysical journal2013
Breaking the radiation damage limit with Cryo-SAXS.
Article in Biophysical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed.
- Advances in the nanostructure characterization of biological hydrogels formed by the prion-like domain of EARLY FLOWERING 3.Acta crystallographica. Section D, Structural biology · 2026Article
- Determination of absolute intramolecular distances in proteins using anomalous X-ray scattering interferometry.Nanoscale · 2025Article
- X-ray driven and intrinsic dynamics in protein gels.Scientific reports · 2023Article
- Resolving molecular diffusion and aggregation of antibody proteins with megahertz X-ray free-electron laser pulses.Nature communications · 2022Article
- Article
- A SAXS-based approach to rationally evaluate radical scavengers - toward eliminating radiation damage in solution and crystallographic studies.Journal of synchrotron radiation · 2021Article
- High-pressure small-angle X-ray scattering cell for biological solutions and soft materials.Journal of applied crystallography · 2021Article
- Advances in integrative structural biology: Towards understanding protein complexes in their cellular context.Computational and structural biotechnology journal · 2021Review
- X-ray photon correlation spectroscopy of protein dynamics at nearly diffraction-limited storage rings.IUCrJ · 2019Article
- The domain swapping of human cystatin C induced by synchrotron radiation.Scientific reports · 2019Article
- Predicting data quality in biological X-ray solution scattering.Acta crystallographica. Section D, Structural biology · 2018Review
- Smaller capillaries improve the small-angle X-ray scattering signal and sample consumption for biomacromolecular solutions.Journal of synchrotron radiation · 2018Article
- Density and electron density of aqueous cryoprotectant solutions at cryogenic temperatures for optimized cryoprotection and diffraction contrast.Acta crystallographica. Section D, Structural biology · 2018Article
- Measuring the Densities of Aqueous Glasses at Cryogenic Temperatures.Journal of visualized experiments : JoVE · 2017Article
- Article
- Development of tools to automate quantitative analysis of radiation damage in SAXS experiments.Journal of synchrotron radiation · 2017Article
- Improved radiation dose efficiency in solution SAXS using a sheath flow sample environment.Acta crystallographica. Section D, Structural biology · 2016Article
- Combined small angle X-ray solution scattering with atomic force microscopy for characterizing radiation damage on biological macromolecules.BMC structural biology · 2016Article
- Actin bundles cross-linked with α-actinin studied by nanobeam X-ray diffraction.European biophysics journal : EBJ · 2016Article
- Thermal contraction of aqueous glycerol and ethylene glycol solutions for optimized protein-crystal cryoprotection.Acta crystallographica. Section D, Structural biology · 2016Article
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7 authors.
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Abstract
Small angle x-ray scattering (SAXS) is a versatile and widely used technique for obtaining low-resolution structures of macromolecules and complexes. SAXS experiments measure molecules in solution, without the need for labeling or crystallization. However, radiation damage currently limits the application of SAXS to molecules that can be produced in microgram quantities; for typical proteins, 10-20 μL of solution at 1 mg/mL is required to accumulate adequate signal before irreversible x-ray damage is observed. Here, we show that cryocooled proteins and nucleic acids can withstand doses at least two orders of magnitude larger than room temperature samples. We demonstrate accurate T = 100 K particle envelope reconstructions from sample volumes as small as 15 nL, a factor of 1000 smaller than in current practice. Cryo-SAXS will thus enable structure determination of difficult-to-express proteins and biologically important, highly radiation-sensitive proteins including light-activated switches and metalloenzymes.
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