Structure Resolution For Free

Resolution is usually reported in Angstroms (1010 meters) for X-ray crystal structures.Most protein structures solved today have a resolution of 1.5 to 2.5 Angstroms, which means the hydrogen atoms are not visible and there is some uncertainty in the precise location of the heavy atoms.

Highest resolution for any protein structure has been achieved for crambin and a high-potential iron-sulphur protein, both at 0.48 Å 5,6, and the perdeuterated form of Pyrococcus furiosus rubredoxin has been refined at 0.59-A… resolution 7.

In cryo-electron microscopy, resolution is typically measured by the Fourier shell correlation (FSC), a three-dimensional extension of the Fourier ring correlation (FRC), which is also known as the spatial frequency correlation function.To measure the FSC, the data needs to be separated into two groups.

Resolution is a measure of the quality of the data that has been collected on the crystal containing the protein or nucleic acid. Most crystallographic-defined structures of proteins fall in between these two extremes.

Since 2010, the average resolution of a cryo-EM structure has improved from 15 Å to about 6 A…, and it is increasingly common for cryo-EM to deliver protein structures in the range of 34 A….

Resolution is measured in Å and can be defined as the minimum spacing (d) of crystal lattice planes that still provide measurable diffraction of X-rays. This term defines the level of detail, or the minimum distance between structural features that can be distinguished in the electron-density maps.

Resolution is a measure of the quality of the data that has been collected on the crystal containing the protein or nucleic acid.Most crystallographic-defined structures of proteins fall in between these two extremes.