State-of-the-art beam lines, instrumentation, techniques, and software for investigating macromolecular structures have been developed by biologists at the Office of Science's four synchrotron radiation facilities, in cooperation with the National Institutes of Health and public and private consortia. These facilities make possible new science, from basic biology to immunology to studies on DNA damage and repair. As an example, more than 600 biologists from universities, pharmaceutical companies, and other national laboratories used seven experimental stations at Brookhaven National Laboratory in the past year to study biological molecules using a technique called X-ray crystallography. The work requires sophisticated detectors to capture the X-rays scattered by atoms in crystallized molecules, and advanced computer software to translate those data into a finished images of molecules. Collectively, the four facilities served about 2,000 unique users in fiscal year 2000, providing high operational efficiency and, in many cases, remote access and automated data collection and reduction.

Scientific Impact: These resources provide the foundation for new initiatives in structural genomics. Recently, studies have shown structures of key components of the infectious agents involved in such diseases as tuberculosis, Lyme disease and AIDS as well as proteins that play central roles in cystic fibrosis and similar disorders."

Social Impact: These state-of-the-art facilities will help scientists from all over the world discover new biological information about the human body, disease agents, and crop plants. Research results may help pharmaceutical and agrichemical companies develop new pharmaceuticals and agricultural products.

Reference: Chang, G.; Spencer, R.H.; Lee,A.T.; Barclay, M.T.; Rees,D.C., "Structure of the MscL Homolog from Mycobacterium tuberculosis: A Gated Mechanosensitive Ion Channel," Science, 282, 2220-2226 (1998).

Kumanan, D. Eswaramoorthy, S.; Luft, B.J.; Koide, S.; Dunn, J.J.; Lawson, C.L.; Swaminathan, S., "Crystal structure of outer surface protein C (OspC) from the Lyme disease spirochete, Borrelia burgdorferi." EMBO Journal, 20, 971-978 (2001).

Rose, R.B.; Craik, C.S.; and Stroud, R.M., "Domain flexibility in retroviral proteases: Structural implications for drug resistant mutations," Biochemistry 37, 2607-2621 (1998).

URL: http://biosync.sdsc.edu/decades.htm

Technical Contact: Dr. Roland Hirsch, Medical Sciences Division, Office of Biological and Environmental Research, 301-903-9009

Press Contact: Jeff Sherwood, DOE Office of Public Affairs, 202-586-5806

SC-Funding Office: Office of Biological and Environmental Research