NIH INSTITUTES SIGN AGREEMENT FOR BIOLOGY RESEARCH AT ARGONNE
18 March 2002 - DOE/Argonne National Laboratory

The National Institute of General Medical Sciences and the National Cancer Institute (NCI) will build the specialized user facility consisting of three new beamlines at the Advanced Photon Source, which produces the nation's most brilliant X-rays for research.

Research at the new beamlines will center on structural studies of biological molecules. "X-ray protein crystallography is a perfect example of the synergy between the health and physical sciences," said J. Murray Gibson, associate laboratory director for the Advanced Photon Source. "We are delighted that the National Cancer Institute and the National Institute of General Medical Sciences are collaborating to build an outstanding new protein crystallography facility at the Advanced Photon Source. They share our confidence that our outstanding X-ray photon source, run by Argonne and the University of Chicago for the Department of Energy, can make a major impact in combating disease."

Dr. Marvin Cassman, director of NIGMS, said that expert structural biologists have been working for two years to develop plans for three state-of-the-art beamlines for protein crystallographic data collection. Cassman praised the work of Drs. Charles Edmonds and John Norvell of NIGMS; Drs. John Sogn and Dinah Singer of NCI; and Drs. Janet Smith of Purdue University and Bob Fischetti of Argonne for their efforts in developing the beamlines.

"The primary motive for the project is to benefit the scientific community by facilitating access to synchrotron beamlines for protein crystallography. This is particularly important as the structural genomics effort at NIGMS begins to pick up speed," Cassman said.

NCI is interested in how the synchrotron facilities will advance the study of cancer at the molecular level. "Given recent advances in our understanding of how protein signaling affects cancer, we are very hopeful that this exciting new technology will aid us in elucidating the structures of proteins and other molecules," said Dr. Andrew C. von Eschenbach, NCI director.

X-ray crystallographers determine the three-dimensional shape of a molecule by blasting a beam of X-rays through a crystallized sample of the molecule and then analyzing the pattern of the scattered beam. X-rays are electromagnetic waves like light, except that their "wavelength" is much smaller and on the scale of an atom. Therefore, unlike light, X-rays are directly sensitive to the atomic structure of objects, and so can be used to identify structure.

Synchrotrons are particularly powerful X-ray sources, more than one million times more brilliant than a medical X-ray machine. This brilliance is needed to solve complex atomic structures, such as biological molecules. Radiation generated by synchrotrons is also "tunable," meaning that scientists can select the wavelengths of X-rays that are optimal for their experiments.

The NIGMS/NCI beamlines will be designed to optimize certain properties of X-rays most useful for specific biological studies. NIGMS and NCI anticipate that these studies will reveal the structures of proteins and other molecules involved in human health and disease. Scientists can use information about these structures to help develop new medicines and diagnostic techniques. In addition to such structural studies, the new synchrotron beamlines can be used for work in cancer biology, immunology and virology, and basic studies in biochemistry, cell biology, molecular biology and biophysics.

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