RT Journal A1 Chance, Mark R. A1 Fiser, Andras A1 Sali, Andrej A1 Pieper, Ursula A1 Eswar, Narayanan A1 Xu, Guiping A1 Fajardo, J. Eduardo A1 Radhakannan, Thirumuruhan A1 Marinkovic, Nebojsa T1 High-Throughput Computational and Experimental Techniques in Structural Genomics JF Genome Research JO Genome Research YR 2004 FD October 15 VO 14 IS 10b SP 2145 OP 2154 DO 10.1101/gr.2537904 UL http://genome.cshlp.org/content/14/10b/2145.abstract AB Structural genomics has as its goal the provision of structural information for all possible ORF sequences through a combination of experimental and computational approaches. The access to genome sequences and cloning resources from an ever-widening array of organisms is driving high-throughput structural studies by the New York Structural Genomics Research Consortium. In this report, we outline the progress of the Consortium in establishing its pipeline for structural genomics, and some of the experimental and bioinformatics efforts leading to structural annotation of proteins. The Consortium has established a pipeline for structural biology studies, automated modeling of ORF sequences using solved (template) structures, and a novel high-throughput approach (metallomics) to examining the metal binding to purified protein targets. The Consortium has so far produced 493 purified proteins from >1077 expression vectors. A total of 95 have resulted in crystal structures, and 81 are deposited in the Protein Data Bank (PDB). Comparative modeling of these structures has generated >40,000 structural models. We also initiated a high-throughput metal analysis of the purified proteins; this has determined that 10%-15% of the targets contain a stoichiometric structural or catalytic transition metal atom. The progress of the structural genomics centers in the U.S. and around the world suggests that the goal of providing useful structural information on most all ORF domains will be realized. This projected resource will provide structural biology information important to understanding the function of most proteins of the cell.