Сравнение методов

	КСНАП	Рентгеновская спектроскопия тонкой структуры поглощения (EXAFS)	РСА
Область	Спектроскопия	Спектроскопия	Спектроскопия
Семейство	Process / pipeline	Process / pipeline	Process / pipeline
Год появления	1975	1971	1954
Автор метода	Peter Lee	Edward Stern	Otto Kratky
Тип	Synchrotron technique	Synchrotron technique	Synchrotron/X-ray technique
Основополагающий источник	Lee, P. A., & Pendry, J. B. (1975). Theory of extended x-ray absorption fine structure. Physical Review B, 11(8), 2795-2811.	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.	Glatter, O., & Kratky, O. (1982). Small Angle X-ray Scattering. Academic Press.
Другие названия	XANES spectroscopy, near-edge X-ray absorption	EXAFS spectroscopy, X-ray absorption spectroscopy	SAXS, small-angle scattering
Связанные	3	3	3
Сводка	X-ray Absorption Near Edge Structure (XANES) is a synchrotron X-ray spectroscopy technique that measures the electronic and geometric structure around a specific atom by analyzing the X-ray absorption spectrum within about 50 eV of an absorption edge. Developed by Lee and Pendry in 1975, XANES is complementary to EXAFS and reveals valence state, local symmetry, and unoccupied orbital structure through near-threshold features and resonances.	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.