Advanced tools for structure determination from low-resolution crystallographic data: Most protein structures are determined through X-ray crystallography. Structure determination and refinement – improving the fit of a model to experimental data – from crystallographic data is challenging and error-prone when the data is low-resolution. Dr. Frank DiMaio has developed tools that combine structure prediction force-fields with low-resolution crystallographic datasets, to develop a method for low-resolution refinement of crystal structures (1). These tools outperform standard refinement methods, and have been used to reveal structural insights into important proteins (2).
1 F. DiMaio*, N. Echols*, J. Headd, T. Terwilliger, P. Adams, D. Baker (2013). Improved protein crystal structures at low resolution by integrated refinement with Phenix and Rosetta. Nat Methods. 10:1102-4.
2 T.I. Brelidze, E.C. Gianulis, F. DiMaio, M.C. Trudeau, W.N. Zagotta (2013). Structure of the C-terminal region of an ERG channel and functional implications. Proceedings of the National Academy of Sciences (PNAS). 110:11648-53.