AB INITIO MODELING BASED ON CRYOEM MAP

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This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Efforts in structural biology have targeted the systematic determination of all protein structures through experimental determination or modeling. In recent years, three-dimensional cryoEM has assumed an increasingly important role in determining the structures of large macromolecular assemblies to intermediate resolutions (6-10¿). While these structures provide a snapshot of the assembly and its components in well-defined functional states, the resolution limits the ability to build accurate structural models. In contrast, sequence-based modeling techniques are capable of producing relatively robust structural models for isolated proteins or domains. We are developing a new computational algorithm to use the cryoEM map as a scoring function to assess thousands of models generated from ab initio modeling.