One goal of structural genomics is to identify novel protein folds. Experimental methods of protein structure determination require proteins that express and/or crystallize well, which may inherently bias the kinds of proteins folds that this experimental data elucidate. A genomic, modeling-based approach such as ab initio modeling may be better able to identify novel protein folds than the experimental approaches because they are not limited by experimental constraints.
Protein function depends on 3-D structure and these 3-D structures are more highly conserved than sequences. Thus, the high-throughput structure determination methods of structural genomics have the potential to inform our understanding of protein functions.  This also has potential implications for drug discovery and protein engineering. Furthermore, every protein that is added to the structural database increases the likelihood that the database will include homologous sequences of other unknown proteins. The Protein Structure Initiative (PSI) is a multifaceted effort funded by the National Institutes of Health with various academic and industrial partners that aims to increase knowledge of protein structure using a structural genomics approach and to improve structure-determination methodology.