Leighton Coates

Leighton Coates

Beam line: BL-11B MANDI

Position: Instrument Scientist

Instrument: Macromolecular Neutron Diffractometer

Group: Energy and the Environment

Facility: Spallation Neutron Source coatesl@ornl.gov


PhD in Neutron Protein Crystallography, the University of Southhampton, UK


Knowing exactly where hydrogen atoms are and how they are transferred between macromolecules, solvent molecules, and substrates is important for understanding many processes. Neutron macromoleular crystallography is a powerful technique for locating hydrogen atoms and is used to provide information on the protonation states of molecules and the nature of bonds involving hydrogen. The ability of neutron diffraction to determine the protonation states of amino acids with and without ligands makes it invaluable in the study of catalytic mechanisms of various molecules. These assets will be of great use in the overall project to help investigate the function of large molecules and assemblies. Dr. Coates came to ORNL after a postdoctoral fellowship as a neutron beam line scientist at Los Alamos National Laboratory from 2005 to 2007 and an earlier postdoctoral fellowship as a researcher in Neutron Protein Crystallography at the University of Southampton, from 2003-2005.

Selected Publications

L. Coates, H.H. Tuan, S. Tomanciek, A. Kovalevsky, M. Mustyakimov, P.T. Erskine, J. Cooper, “The Catalytic Mechanism of an Aspartic Proteinase Explored with Neutron and X-ray Diffraction,” JACS 130 7235–7237 (2008)

K. Katz, X. Li, H. L. Carrell, B. L. Hanson, P. Langan, L. Coates, B. P. Schoenborn, J. P. Glusker, and G.J. Bunick, “Locating active-site hydrogen atoms in D-xylose isomerase: time-of-flight neutron diffraction,” PNAS 103 8342-8347 (2006)

B. Bennett, P. Langan, L. Coates, and C. Dealwis, “Complementary neutron and ultrahigh X-ray diffraction studies of Escherichia coli Dihydrofolate reductase complexed with methotrexate,” PNAS 103 18493-18498 (2006)

L. Coates, P.T. Erskine, S.P. Wood, D.A.A. Myles, and J.B. Cooper, “A Neutron Laue Diffraction Study of Endothiapepsin: Implications for the Aspartic Proteinase,” Mechanism Biochemistry 40 13149 (2001)