F A C U L T Y   P R O F I L E 

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University Professor and the Violin Family Professor of Physiology and Cellular Biophysics

Macromolecular structure with an aim toward in-depth understanding of biological activity.


Current Research

Wayne A. Hendrickson is the Violin Family Professor of Physiology and Cellular Biophysics as well as being a University Professor and a member of the Department of Biochemistry and Molecular Biophysics at Columbia University. He also holds the positions of Chief Life Scientist for Photon Sciences at Brookhaven National Laboratory and Scientific Director of the New York Structural Biology Center.

Research in Dr. Hendrickson's laboratory focuses on the structure and function of biological molecules. He and his colleagues use x-ray crystallography to study molecular properties in atomic detail. By analyzing x-ray beams diffracted from crystals, they are able to reconstruct images of crystallized molecules. Their advances in diffraction methods (notably, stereochemically restrained refinement, the multiwavelength-anomalous-diffraction (MAD) method, selenomethionyl proteins, and synchrotron instrumentation) have been instrumental in the emergence of structural biology as a major force in modern biology and molecular medicine. They use this technology themselves in investigations on membrane receptors and cellular signaling, on viral proteins and HIV infection, on molecular chaperones and protein folding, and in structural genomics of membrane proteins.

Dr. Hendrickson has published numerous research articles and related reviews. He serves on advisory bodies for various scientific organizations. He is a founding editor of Current Opinion in Structural Biology and of Structure, and he was a founder of SGX Pharmaceuticals. His honors include the Aminoff Prize of the Royal Swedish Academy of Sciences, the Gairdner International Award, and the Harvey Prize of the Technion – Israel Institute of Technology. He is a fellow of the American Academy of Arts and Sciences and a member of the National Academy of Sciences.

Selected Publications

F. Fiumara, L. Fioriti, E.R. Kandel and W.A. Hendrickson, Essential Role of Coiled-Coils for Aggregation and Activity of Q/N-rich Prions and PolyQ Proteins. Cell 143,1121-1135 (2010).

Y.-H. Chen, L. Hu, M. Punta, R. Bruni, B. Hillerich, B. Kloss, B. Rost, J. Love, S.A. Siegelbaum and W.A. Hendrickson, Homologue Structure of the SLAC1 Anion Channel for Closing Stomata in Leaves. Nature 467, 1074-1080 (2010).

M.N. Collins and W.A. Hendrickson, Structural Characterization of the Boca/Mesd Maturation Factors for LDL-Receptor-Type β Propeller Domains. Structure 19, 324-336 (2011).

Q. Liu, Z. Zhang and W.A. Hendrickson, Multi-crystal Anomalous Diffraction for Low Resolution Macromolecular Phasing. Acta Cryst. D 67, 45-59 (2011).

J.O. Moore and W.A. Hendrickson, An Asymmetry-to-Symmetry Switch in Signal Transmission by the Histidine Kinase Receptor for TMAO. Structure 20, 729-741 (2012).

Q. Liu, T. Dahmane, Z. Zhang, Z. Assur, J. Brasch, L. Shapiro, F. Mancia and W.A. Hendrickson. Structures from Anomalous Diffraction Data of Native Biological Macromolecules. Science 336, 1033-1037 (2012).

A. Korkut and W.A. Hendrickson, Structural Plasticity and Conformational Transitions of HIV Envelope Protein gp120. PLoS ONE 7, e52170 (2012).

R. Qi, E.B. Sarbeng, Q. Liu, K.Q. Le, X. Xu, H. Xu, J. Yang, J.L. Wong, C. Vorvis, W.A. Hendrickson, L. Zhou and Q. Liu. Allosteric Opening of the Polypeptide-binding Site when an Hsp70 Binds ATP. Nat. Struct. Mol. Biol. 20, 900-907 (2013).

Q. Liu, Q. Liu and W.A. Hendrickson, Robust Structural Analysis of Native Biological Macromolecules from Multi-crystal Anomalous Diffraction Data. Acta Crystallor. D 69, 1314-1332 (2013).

J.M. LaLonde, M. Le-Khac, D.M. Jones, J.R. Courter, J. Park, A. Schön, A.M. Princiotto, X. Wu, J.R. Mascola, E. Freire, J. Sodroski, N. Madani, W.A. Hendrickson and A.B. Smith, III, Structure-Based Optimization of a Small Molecule HIV-1 Entry Inhibitor Exploiting X-ray and Thermodynamic Characterization. ACS Med Chem. Lett.4, 338-343 (2013).