Our goal is to develop a high-throughput and cost-effective structure pipeline and to utilize it to determine novel protein folds and to explore protein structure/function relationships.
We have applied this approach to the extensive study of the thermophilic bacterium Thermotoga maritima, as well as, targets from mouse and over 100 bacterial genomes.
Our technologies have allowed us to perform comprehensive structural studies of these proteomes. To date, these efforts have resulted in over 500 novel protein structures at a current rate of ~175 structures per year.
Furthermore, we have used structural data and performed biochemical assays to validate predicted activities and determine function for numerous targets for which no function could be predicted.