This subproject is one of many research subprojects utilizing theresources provided by a Center grant funded by NIH/NCRR. The subproject andinvestigator (PI) may have received primary funding from another NIH source,and thus could be represented in other CRISP entries. The institution listed isfor the Center, which is not necessarily the institution for the investigator.We have developed a computational method to enforce spatial restraints from solution x-ray scattering data in the modeling of multi-domain proteins and protein complexes. Available high-resolution structures of domains or components can be included in different conformations, based on structures of respective homologues, in our method. It optimizes the atomic coordinates of the rigid fragments and flexible linkers, if present, with respect to a solution scattering penalty, stereochemistry, steric clashes, and geometric symmetries, if specified. An ensemble of models is built and subsequently clustered to determine the major conformations that are consistent with the given data. We have demonstrated the effectiveness of our method using simulated examples and an experimental case, the homotetramer glucose isomerase, whose scattering curves were recorded on BL4-2.
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