I have over 35 years experience in macromolecular crystallography. I began my career in 1980 isolating and purifying the protein neurophysin (neurophysin is involved in the storage of the hormones oxytocin and vasopressin) from porcine posterior pituitary glands for crystallization trials. As part of these studies I also synthesized the hormone analogues Phe-Tyr amide and Tyr-Phe amide in the laboratory of Klaus Hofmann at the University of Pittsburgh, since these peptides were needed for the crystallization trials. Once I had crystals I learned an important lesson - data quality depends both on the crystal and the X-ray source. Because of this I have over 30 years experience in managing/maintaining X-ray facilities at the University of Pittsburgh, the Institute of Molecular Biology, Academia Sinica (IMB), Taiwan and the University of Georgia.
Although my formal training was small molecule crystallography my post doctoral work with B.C. Wang work gave me a solid foundation in all phases of the macromolecular crystal structure determination process from producing and purifying protein to validating the final refined protein structure. During this time BC Wang developed his solvent flattening process that revolutionized the field. His ISAS method relying on single-wavelength anomalous scattering data reduced the need for Multiple ISOMORPHOUS heavy atom derivatives since all necessary data could, in most cases be collected on a single crystal containing an anomalous scatterer (introduced by soaking or by seleomethionine labeling). Under BC's watchful eye and using cocrystals of a neurophysin complexed with p-iodo Phe-Tyr amide Liqing Chen and I were able to phase the first ISAS structure. Today a majority of de novo protein structures are determined from single-wavelength anomalous scattering data.
To be continued ...
1971-1974 Benedictine College, Atchison, KS B.A. Chemistry
1975-1980 Rutgers University, Newark, NJ Ph.D. Physical Chemistry
1980-1986 University of Pittsburgh, Pittsburgh, PA Postdoctoral Fellow Crystallography