Severe acute respiratory syndrome (SARS) emerged as the first severe and readily transmissible new disease of the 21st century. The debilitating pneumonia-like disease is caused by coronavirus, which caused 916 deaths out of about 8,400 reported cases. Scientists from The Scripps Research Institute in California have embarked on an ambitious program to characterize the structure and function of all the proteins built or used by SARS. Taking advantage of advances in robotics and automation at Stanford Synchrotron Radiation Laboratory as well as other new tools, the scientists ultimately hope to rapidly characterize the complete protein sets of emerging disease organisms and then provide structure information to design inhibitors to stop the organisms.

In a recent paper, the group reported the structure of a part of one SARS protein, one of the first resulting from the Scripps project, and with the data measured on SSRL's BL11-1. The high resolution structure is providing insights into mechanisms the virus uses to replicate itself.

To learn more about this research see the full scientific highlight at:
http://www-ssrl.slac.stanford.edu/research/highlights_archive/nsp3.html

Saikatendu KS, Joseph JS, Subramanian V, Clayton T, Griffith M, Moy K, Velasquez J, Neuman BW, Buchmeier MJ, Stevens RC, Kuhn P (2005). Structural basis of severe acute respiratory syndrome coronavirus ADP-ribose-1''-phosphate dephosphorylation by a conserved domain of nsP3. Structure. 13, 1665-1675.