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Resolution. Resolution is a measure of the quality of the data that has been collected on the crystal containing the protein or nucleic acid. Lower resolution structures, with resolution of 3 Å or higher, show only the basic contours of the protein chain, and the atomic structure must be inferred.
In X-ray crystallography, resolution is the smallest distance between crystal lattice planes that is resolved in the diffraction pattern. High numeric values of resolution, such as 4 Å, mean poor resolution, while low numeric values, such as 1.5 A, mean good resolution.
Resolution. Resolution is a measure of the quality of the data that has been collected on the crystal containing the protein or nucleic acid. So resolution is a measure of the level of detail present in the diffraction pattern and the level of detail that will be seen when the electron density map is calculated.
On average, at 2.0 A resolution one water molecule per residue is included in the model, while at 1.0 A resolution about 1.6-1.7 are crystallographically located.
Free R (also called Free) “is generally considered the most useful global measure of model-to-data agreement”. It is a statistical quantity introduced in 1992 by Axel T. Bringer to assess the quality of a model from X-ray crystallographic data.
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