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| EXAFS× | SAXS× | |
|---|---|---|
| Dziedzina | Spektroskopia | Spektroskopia |
| Rodzina | Process / pipeline | Process / pipeline |
| Rok powstania≠ | 1971 | 1954 |
| Twórca≠ | Edward Stern | Otto Kratky |
| Typ≠ | Synchrotron technique | Synchrotron/X-ray technique |
| Źródło pierwotne≠ | Sayers, D. E., Stern, E. A., & Lytle, F. W. (1971). New technique for investigating noncrystalline structures: Fourier analysis of the extended X-ray absorption fine structure. Physical Review Letters, 27(18), 1204-1207. DOI ↗ | Glatter, O., & Kratky, O. (1982). Small Angle X-ray Scattering. Academic Press. link ↗ |
| Inne nazwy | EXAFS spectroscopy, X-ray absorption spectroscopy | SAXS, small-angle scattering |
| Pokrewne | 3 | 3 |
| Podsumowanie≠ | Extended X-ray Absorption Fine Structure (EXAFS) is a synchrotron-based X-ray spectroscopy technique that measures the local geometric and electronic structure around a specific atom in any material, crystal or amorphous. Discovered by Sayers, Stern, and Lytle in 1971, EXAFS reveals interatomic distances, coordination numbers, and disorder in the atomic environment by analyzing oscillations in the X-ray absorption spectrum above an absorption edge. | Small-Angle X-ray Scattering (SAXS) is a solution-phase X-ray scattering technique that measures the overall shape and size of macromolecules and nanoparticles by analyzing scattering intensity at low angles (0.1-10 degrees). Developed by Kratky and colleagues in the 1950s, SAXS provides information about molecular radius, aggregation state, and overall shape without requiring crystallization or fixing, making it ideal for studying native protein conformations and dynamics. |
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