October 5, 2006
Stanford University's Synchrotron Radiation Laboratory at SLAC contributes to 2006 Nobel Prize in Chemistry
By Kelen Tuttle
Roger D. Kornberg, who won this year's Nobel Prize in Chemistry, carried out a significant part of the research leading to this prize at the Stanford Synchrotron Radiation Laboratory (SSRL), a Department of Energy (DOE)-supported research facility located at the Stanford Linear Accelerator Center (SLAC).
"Congratulations to Dr. Roger Kornberg for his outstanding research on determining how the RNA molecule turns DNA's genetic blueprint into working proteins, which is important to all of us," said DOE Under Secretary for Science Raymond L. Orbach.
Kornberg, a professor in the Structural Biology Department at Stanford, also carried out research at the Advanced Light Source, another DOE-funded synchrotron light source located at the Lawrence Berkeley National Laboratory.
"I am pleased and proud that the experimental work that led to Dr. Kornberg's Nobel Prize award took place at two Department of Energy-funded synchrotron radiation laboratories," Orbach said. "I congratulate all the staff at these two world-class laboratories on their high-quality work."
Kornberg was the first to create an actual picture of how transcription works at a molecular level in the important group of organisms called eukaryotes (organisms whose cells have a well-defined nucleus). Humans and other mammals are included in this group, as is ordinary yeast.
"We could not have solved the problem that was noted in the Nobel Prize announcement without the exceptional facilities given to us by SLAC," Kornberg said. "They were indispensable."
For cells to produce working proteinsa process necessary for lifeinformation stored in DNA must first be transcribed into a form readable by the cell's internal machinery. Kornberg's studies have provided an understanding at the atomic level of how the process of transcription occurs and also how it is controlled. Because the regulation of transcription underlies all aspects of cellular metabolism, Kornberg's research also helps explain how the process sometimes goes awry, leading to birth defects, cancer and other diseases.
Since the early 1990s, Kornberg has studied transcription at SSRL's beamlines 9-2 and 11-1. By passing the lab's extremely bright X-rays through crystallized proteins and watching how the X-rays scattered, Kornberg revealed the three-dimensional atomic structure of proteins in high resolution. The high level of detail allowed Kornberg to view the complex structures that make up proteins and offered the first real understanding of the defining events of transcription.
"We are very pleased that the magnificent structural work of Roger Kornberg and his colleagues was significantly enabled by synchrotron X-rays at SSRL," said SLAC Deputy Director Keith Hodgson. "These studies offer our most detailed glimpse into the inner workings of one of nature's most remarkable molecular machines."
The SSRL Structural Molecular Biology Program and the beamlines on which much of the crystallography work was performed are supported by the DOE, Office of Biological and Environmental Research; the National Institutes of Health; the National Center for Research Resources and the National Institute of General Medical Sciences. SSRL operations are supported by the DOE Office of Basic Energy Sciences.
A photo of Kornberg is available on the web at http://newsphotos.stanford.edu.