Protein structure determination to atomic accuracy from cryoEM density using Rosetta

Recent advances in technology have made determination of cryoEM single particle reconstructions at 3-5Å resolution routine, even for relatively small protein complexes with low symmetry. While this “near-atomic resolution” data provides key structural information, determination of an atomic model from such maps is difficult and error prone. I will describe the developments my lab has made in advancing the Rosetta protein structure prediction methodology to bridge this “resolution gap,” allowing accurate determination of atomic details from such sources of data. I will describe the tools our lab has developed for automated de novo model building, model completion, and all atom refinement, as well as ongoing efforts at extending our approach to even lower resolution sources of data.