The Howard Hughes Medical Institute (HHMI), a philanthropy that is one of the world's leading biomedical research organizations, will spend $8.05 million for the construction and operation of two new "superbend" beamlines at the Advanced Light Source (ALS) of the U.S. Department of Energy's Lawrence Berkeley National Laboratory (Berkeley Lab). The beamlines will generate the high-energy or "hard" x-rays that are ideal for protein crystallography research.
"The Hughes Institute is pleased to be teaming up with the Lawrence Berkeley National Laboratory," said Thomas R. Cech, the president-designate of HHMI who takes office on January 1, 2000. "The need for more such state-of-the-art facilities is growing because of the unsurpassed power of x-ray crystallography. The detailed 3-D views of biomedically important molecules that this technique yields provide a powerful framework for understanding how molecules function and interact."
Said Berkeley Lab director Charles V. Shank, "This is the single largest investment in the ALS ever made by an organization outside of DOE. It reflects the growing importance of x-ray crystallography as a critical tool for the biomedical research community and recognizes the success and promise of the ALS in identifying and characterizing proteins."
As the Human Genome Project approaches completion, the next big steps are to identify the proteins that human DNA codes for and find out what those proteins do. The key to understanding a protein's function is to determine its three-dimensional structure and x-ray crystallography -- using a synchrotron light source like the ALS -- is one of the main techniques for accomplishing this. In x-ray crystallography, a beam of x-rays sent through a protein crystal creates a set of diffraction patterns that can be translated by computer into 3-D images with atomic-scale resolution.
The ALS houses one of the top experimental facilities in the world for determining protein crys
Contact: Lynn Yarris
DOE/Lawrence Berkeley National Laboratory