ArticleCommunications biology2023
Form factor determination of biological molecules with X-ray free electron laser small-angle scattering (XFEL-SAS).
Article in Communications biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed.
- Ultrafast time-resolved small-angle X-ray scattering setup on the FemtoMAX beamline.Journal of synchrotron radiation · 2026Article
- Native mass spectrometry meets X-rays for the elucidation of protein structures.Biochemical Society transactions · 2026Review
- Absolute scaling of small- and wide-angle X-ray scattering images recorded with short duration X-ray pulses on a large area fiber-taper X-ray detector.Journal of synchrotron radiation · 2026Article
- Signal extraction in SWAXS data for the compact X-ray light sources: a machine learning approach.Scientific reports · 2026Article
- Superstability of micrometre jets surrounded by a polymeric shell.Journal of applied crystallography · 2025Article
- Advances in microfluidic mixers for time-resolved structural biology with X-rays.Biophysical reviews · 2025Review
- Controlling Protein Immobilization over Poly(3-hydroxybutyrate) Microparticles Using Substrate Binding Domain from PHA Depolymerase.Biomacromolecules · 2025Article
- Time-resolved small-angle X-ray scattering system development for the biological macromolecules at SACLA: A pilot study.Biophysics and physicobiology · 2025Article
- Analyzing aptamer structure and interactions: in silico modelling and instrumental methods.Biophysical reviews · 2024Review
- Thinner than a knife's edge: 3D-printed liquid sheet jet technology for solution phase XFEL experiments.IUCrJ · 2023Article
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40 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Free-electron lasers (FEL) are revolutionizing X-ray-based structural biology methods. While protein crystallography is already routinely performed at FELs, Small Angle X-ray Scattering (SAXS) studies of biological macromolecules are not as prevalent. SAXS allows the study of the shape and overall structure of proteins and nucleic acids in solution, in a quasi-native environment. In solution, chemical and biophysical parameters that have an influence on the structure and dynamics of molecules can be varied and their effect on conformational changes can be monitored in time-resolved XFEL and SAXS experiments. We report here the collection of scattering form factors of proteins in solution using FEL X-rays. The form factors correspond to the scattering signal of the protein ensemble alone; the scattering contributions from the solvent and the instrument are separately measured and accurately subtracted. The experiment was done using a liquid jet for sample delivery. These results pave the way for time-resolved studies and measurements from dilute samples, capitalizing on the intense and short FEL X-ray pulses.
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