Wayne A. Hendrickson

Wayne Hendrickson's pioneering studies of the anomalous dispersion effect have established this technique as the method of choice for determining protein crystal structures in as rapid and straightforward manner as possible and has made the concept of structural genomics an experimental reality. In addition to his central role in the development of multi-wavelength anomalous diffraction (MAD) methods, he was also a pioneer in the development of computer programs that are used to build and refine atomic models for proteins on the basis of X-ray diffraction measurements. His contributions to methodology are complemented by his determination of the first structure of a tyrosine kinase and the structure of the HIV protein, gp120, in complex with the CD4 receptor and a neutralizing human antibody.

Wayne Hendrickson was born in Spring Valley, Wisconsin, he received his BA in Physics and Biology at the University of Wisconsin and his PhD in Biophysics from Johns Hopkins University, followed by postdoctoral work at the Naval Research Laboratory in Washington. In 1984, he joined the faculty of the Department of Biochemistry and Molecular Biophysics at Columbia. Wayne Hendrickson is a member of the National Academy of Sciences and is a recipient of several awards including the Alexander Hollaender Award of the National Academy of Sciences, the Christian B. Anfinsen Award of the Protein Society, the Merit Award of the National Institutes of Health, the Academy Medal, New York Academy of Medicine (2003), the Paul Janssen Prize (with M. G. Rossmann), Rutgers University (2004), and the Harvery Prize, Technion - Israel Institute of Technology (2004).