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In X-ray crystallography, resolution is a measure of the resolvability or precision in the electron density map of a molecule. Resolution is usually reported in Angstroms (Å, 10 –10 meters) for X-ray crystal structures. The smaller the number, the better the degree of atomic resolution.
Experimental approaches of determining the structure of nucleic acids, such as RNA and DNA, can be largely classified into biophysical and biochemical methods. Biophysical methods use the fundamental physical properties of molecules for structure determination, including X-ray crystallography, NMR and cryo-EM.
It is used in the fields of X-ray crystallography and nuclear magnetic resonance spectroscopy of proteins (NMR) analysis. [1] X-PLOR is a highly sophisticated program that provides an interface between theoretical foundations and experimental data in structural biology, with specific emphasis on X-ray crystallography and nuclear magnetic ...
The first of these is by X-ray crystallography, starting in 1958 when the crystal structure of myoglobin was determined. The second method is by NMR, which began in the 1980s when Kurt Wüthrich outlined the framework for NMR structure determination of proteins and solved the structure of small globular proteins. [5]
A powder X-ray diffractometer in motion. X-ray crystallography is the experimental science of determining the atomic and molecular structure of a crystal, in which the crystalline structure causes a beam of incident X-rays to diffract in specific directions.
A set of conformations, determined by NMR or X-ray crystallography may be a better representation of the experimental data of a protein than a unique conformation. [23] The utility of a model will be given, at least in part, by the degree of accuracy and precision of the model.
Macromolecular crystallography was preceded by the older field of small-molecule x-ray crystallography (for structures with less than a few hundred atoms). Small-molecule diffraction data extends to much higher resolution than feasible for macromolecules, and has a very clean mathematical relationship between the data and the atomic model.
[3] [4] Contrary to X-ray, single crystals are not necessary with solid-state NMR and structural information can be obtained from high-resolution spectra of disordered solids. [5] E.g. polymorphism is an area of interest for NMR crystallography since this is encountered occasionally (and may often be previously undiscovered) in organic ...