Quality control of three-dimensional structures of macromolecules is a critical step to ensure the integrity of structural biology data, especially those produced by structural genomics centers. Whereas the Protein Data Bank (PDB) has proven to be a remarkable success overall, the inconsistent quality of structures reveals a lack of universal standards for structure/deposit validation. Here, we review the state-of-the-art methods used in macromolecular structure validation, focusing on validation of structures determined by X-ray crystallography. We describe some general protocols used in the rebuilding and re-refinement of problematic structural models. We also briefly discuss some frontier areas of structure validation, including refinement of protein-ligand complexes, automation of structure redetermination, and the use of NMR structures and computational models to solve X-ray crystal structures by molecular replacement. © 2014 Springer Science+Business Media, LLC.
CITATION STYLE
Domagalski, M. J., Zheng, H., Zimmerman, M. D., Dauter, Z., Wlodawer, A., & Minor, W. (2014). The quality and validation of structures from structural genomics. Methods in Molecular Biology, 1091, 297–314. https://doi.org/10.1007/978-1-62703-691-7_21
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