To identify the structures of the full complement of proteins that make up these two "minimal organisms," Kim and his colleagues will primarily use x-ray crystallography, backed by nuclear magnetic resonance and computation. In x-ray crystallography, a beam of x-rays is sent through a protein's crystal. The crystal's atoms cause the incoming photons to be scattered, creating a diffraction pattern that computers can translate into a 3-D image of the protein's structure. Kim and his colleagues will have access to the Berkeley Center for Structural Biology which features one of the world's premier x-ray beamlines for protein crystallography at Berkeley Lab's Advanced Light Source (ALS). The ALS is an electron synchrotron that produces beams of x-rays and ultraviolet light for scientific research, which are a hundred million times brighter than those from the best x-ray tubes. This high brightness reduces the time required to collect a complete set of data for a single protein from what had once been months or even years using an x-ray tube, to a matter of weeks, days, or even hours.
"The use of a synchrotron radiation source such as the ALS can dramatically decrease the time required to solve novel protein structures," Kim has said. "It makes a clear and compelling case that protein crystallography can provide a foundation for structural genomics."
As a major part of their effort, Kim and his collaborators will look to reduce t
'"/>
Contact: Lynn Yarris
lcyarris@lbl.gov
510-486-5375
DOE/Lawrence Berkeley National Laboratory
26-Sep-2000