Resolution-by-proxy: a simple measure for assessing and comparing the overall quality of NMR protein structures.
 

From Mendeley Biomolecular NMR group:

Resolution-by-proxy: a simple measure for assessing and comparing the overall quality of NMR protein structures.

Journal of biomolecular NMR (2012). Mark Berjanskii, Jianjun Zhou, Yongjie Liang, Guohui Lin, David S Wishart et al.


In protein X-ray crystallography, resolution is often used as a good indicator of structural quality. Diffraction resolution of protein crystals correlates well with the number of X-ray observables that are used in structure generation and, therefore, with protein coordinate errors. In protein NMR, there is no parameter identical to X-ray resolution. Instead, resolution is often used as a synonym of NMR model quality. Resolution of NMR structures is often deduced from ensemble precision, torsion angle normality and number of distance restraints per residue. The lack of common techniques to assess the resolution of X-ray and NMR structures complicates the comparison of structures solved by these two methods. This problem is sometimes approached by calculating "equivalent resolution" from structure quality metrics. However, existing protocols do not offer a comprehensive assessment of protein structure as they calculate equivalent resolution from a relatively small number (