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Quality of protein crystal structures

Acta Cryst. (2007). D63, 941–950 [doi:10.1107/S0907444907033847]

[protein structure quality]
A method that will allow for comparison of crystallographic models deposited in the Protein Data Bank (PDB) (accounting for differences in resolution, protein size, sequence novelty and deposition date) has been developed. Analysis of structures reveals interesting features that indicate that the quality of deposited models in the PDB has not changed over time and the average quality of structures deposited by the structural genomics groups is better. A significant observation is the larger proportion of poor-quality structures published in general-science journals.
E.N. Brown and S. Ramaswamy