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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 |
