Prediction of Symmetric Assemblies: Symmetry is ubiquitous in naturally occurring proteins. IPD researchers have developed efficient methods for modeling and predicting symmetric protein assemblies(1). Combining these methods with experimental data allows for accurate determination of symmetric structures from sparse experimental data. Accurate recapitulation of the energetics of crystal lattice formation is critical in low-resolution crystallographic refinement. This work shows that by taking into account the energetics of proteins in crystal lattices, one can explain apparent shortcomings in molecular force fields(2).
1. F. DiMaio, A. Leaver-Fay, P. Bradley, D. Baker, I. André. (2011) Modeling symmetric macromolecular structures in Rosetta3. PLoS One. 6:e20450.
2. M. Tyka, D. Keedy, I. André, F. DiMaio, Y. Song, D. Richardson, J. Richardson and D. Baker (2010). Alternate states of proteins revealed by detailed energy landscape mapping. Journal of Molecular Biology. 405:607-18.