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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.
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 ...
Nucleic acid NMR is the use of NMR spectroscopy to obtain information about the structure and dynamics of nucleic acid molecules, such as DNA or RNA. As of 2003, nearly half of all known RNA structures had been determined by NMR spectroscopy. [2] Nucleic acid NMR uses similar techniques as protein NMR, but has several differences.
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]
The series contains books that covers analysis methods and the mathematical procedures for determining organic structure through x-ray crystallography, electron diffraction, and neutron diffraction. The International tables are focused on procedures, techniques and descriptions and do not list the physical properties of individual crystals ...
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.
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 common goal of these investigations is to obtain high resolution 3-dimensional structures of the protein, similar to what can be achieved by X-ray crystallography. In contrast to X-ray crystallography, NMR spectroscopy is usually limited to proteins smaller than 35 kDa, although larger structures have been solved. NMR spectroscopy is often ...