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. Exploration of protein folds by X-ray crystallography is a basis of modern structural biology. It is generally believed that functionally relevant proteins form a limited number of folding families which can be mapped by the high-throughput methods of protein crystallography and NMR. The C. elegans genome, with approximately 19000 predicted genes, provides opportunity for structural studies of a small eukaryotic organism and has been selected as a target by the Southeast Collaboratory for Structural Genomics. Although a significant progress has been made in production and crystallization of the C. elegans proteins, availability of the synchrotron beam time is still limited. We propose a series of diffraction experiments directed towards MAD/SAD phasing of the novel protein structures from C. elegans. A majority of the proteins will be either derivatized by heavy atom reagents or produced as selenomethionine/selenocysteine variants. Based on the current production, we estimate data collection for 10-15 proteins.
Showing the most recent 10 out of 604 publications
