手法を比較

	EXAFS	ATR-FTIR	X線小角散乱法（SAXS）
分野	分光学	分光学	分光学
系統	Process / pipeline	Process / pipeline	Process / pipeline
提唱年	1971	1961	1954
提唱者	Edward Stern	Joop Fahrenfort	Otto Kratky
種類	Synchrotron technique	Vibrational spectroscopy technique	Synchrotron/X-ray technique
原典	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.	Harrick, N. J. (1960). Study of physics of internal reflection from metals. Journal of Physics and Chemistry of Solids, 13(2), 143-155.	Glatter, O., & Kratky, O. (1982). Small Angle X-ray Scattering. Academic Press.
別名	EXAFS spectroscopy, X-ray absorption spectroscopy	ATR-IR, attenuated total reflectance, FTIR spectroscopy	SAXS, small-angle scattering
関連	3	3	3
概要	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.	Attenuated Total Reflectance (ATR) Fourier Transform Infrared (FTIR) spectroscopy is a variant of conventional FTIR that measures infrared absorption through evanescent-wave interrogation of samples in direct contact with a high-refractive-index crystal. Developed by Harrick and Fahrenfort in the 1960s, ATR-FTIR is now the dominant form of FTIR spectroscopy, enabling rapid, non-destructive characterization of organic compounds, polymers, coatings, and biological materials without extensive sample preparation.	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.