Number 187 (Story #3), July 11, 1994 by Phillip F. Schewe and Ben Stein THREEFOLD INCREASED DETAIL IN THE STRUCTURE OF A BIOMOLECULE was obtained when researchers applied a combination of several powerful techniques to x-ray crystallography. Wladek Minor (317-494-0879) of Purdue University and his colleagues used the Cornell High Energy Synchrotron Source to determine the atomic structure of crystallized L- 1 lipoxygenase enzyme, a protein involved in polyunsaturated fatty acid metabolism in both mammals and plants. The synchrotron radiation's high intensity, combined with a special CCD detector, allowed the researchers to obtain data rapidly and with a very high signal-to-noise ratio. Cooling the crystal to near-liquid nitrogen temperatures preserved the crystalline order for hours of synchrotron beam exposure, permitting three times the number of observations than the best previous data set for this protein. Analysis of the data yielded crystal structure information with a resolution of 1.4 Angstroms, the best yet for such a large protein (containing 839 amino acids). Minor says this combination of techniques can be applied to learn new structural details of other proteins and viruses. (Paper at the meeting of the American Crystallographic Association in Atlanta, June 27-July 1.)