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Team Solves X-ray Structure Of Powerful Enzyme

of one member of the enzyme family exactly as it is found in its natural state. The large, accurate quantities were required for collaborator James Hurley of the NIH to determine the three-dimensional X-ray crystal structure of the enzyme. The technique entails growing a crystal of the enzyme, taking an X-ray picture of it and then processing the X-ray image through a computer.

"Understanding the structure of the enzyme at the molecular level, as we have done with this X-ray crystallography, will help scientists figure out how to manipulate it," said Anderson. "Using these studies as a foundation, we will be able to modify the enzyme, either genetically or by developing therapeutic drugs that can block the generation of second messengers."

Anderson said the next step for his laboratory will be to use the structural information to study the way the enzymes control activities that result in functions such as cell growth and movement.


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Contact: Dian Land
dianland@macc.wisc.edu
(608) 263-9893
University of Wisconsin-Madison
28-Sep-1998


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