Leighton Coates

STS Instrument Systems Science and Technology Manager

Leighton is involved in the development of instrumentation for the Second Target Station (STS) of the Spallation Neutron Source (SNS).  His early Ph.D. work at the University of Southampton (UK) involved single-crystal neutron and X-ray diffraction work on the catalytic mechanism of aspartic proteinases. Following a relocation from the UK to the USA in 2005, he started to work as a postdoctoral researcher at the Los Alamos Neutron Scattering Center (LANSCE) as a beamline scientist at the protein crystallography station (PCS). The PCS was a proof of principle pulsed source neutron beamline available to the crystallographic user community by peer review. In 2007 Leighton moved to Oak Ridge National Laboratory (ORNL) to design and construct a macromolecular neutron diffractometer (MaNDi) at the Spallation neutron source (SNS), which has enabled neutron protein crystallography to study smaller crystals with larger unit cell dimensions. The design, construction, and commissioning of this unique beamline took a total of seven years to complete and has provided a unique resource and capability to the US crystallographic community. In 2020 he moved to the STS to coordinate the physics design and optimization of neutron instrumentation.  

Leighton currently serves the crystallographic community as the president of the Pittsburgh Diffraction Society (PDS). That is a not-for-profit organization that promotes fundamental and applied diffraction as well as the exchange of ideas and information concerning such research. The PDS was founded by Professor Surain S. Sidhu, who organized the first Pittsburgh Diffraction Conference in 1943. Since that time, the PDS has sponsored an annual conference which is held annually, returning to Pittsburgh, Pennsylvania, every five years. 

Selected Publications 

Azadmanesh, J.,  Lutz, W.  E,  Coates, L., Weiss, K.L., Borgstahl, G. E. O. Direct detection of coupled proton and electron transfers in human manganese superoxide dismutase Nature Communications (2021). https://www.nature.com/articles/s41467-021-22290-1

Kneller, D. W., Phillips, G., Weiss, K.L., Zhang, Q., Coates, L., Kovalevsky, A. Direct Observation of Protonation State Modulation in SARS-CoV-2 Main Protease upon Inhibitor Binding with Neutron Crystallography (2021) J. Med. Chem. https://doi.org/10.1021/acs.jmedchem.1c00058

Kneller, D.W., Phillips, G., O’Neill, H.M.,  Jedrzejczak, R., Stols, L.,  Langan, P.,  Joachimiak, A., Coates, L., Kovalevsky. A.Structural plasticity of SARS-CoV-2 3CL Mpro active site cavity revealed by room temperature X-ray crystallography (2020) Nature Communications volume 11, Article number: 3202

Langan, P.S., Vandavasi, V.G., Weiss, K.L., Afonine, P.V., Omari, K.E., Duman, R., Wagner, A., Coates,  L. Anomalous X-ray Diffraction Studies of Ion Transport in K+channels. (2018) Nature Communications 9:4540 | DOI: 10.1038/s41467-018-06957-w

Sullivan, B.,  Archibald, R.,  Langan, P.S.,   Dobbek, H., Bommer,  M., McFeeters,  M.L, Coates, L., Wang,  X.P., Gallmeier,  F., Carpenter, J.M.,  Lynch V., Langan, P. Improving the Accuracy and Resolution of Neutron Crystallographic Data by 3D Profile Fitting of Bragg Peaks in Reciprocal Space. (2018) Acta Crystallographica Section D: Structural Biology 74, 11, 1085-1095

Li, Z., Zhang, X., Wang, Q., Li, C., Zhang, N., Zhang, X., Xu, B., Ma, B., Schrader, T.E., Coates, L., Kovalevsky, A., Huang, Y., Wan, Q. Understanding the pH-Dependent Reaction Mechanism of a Glycoside Hydrolase Using High-Resolution X-ray and Neutron Crystallography (2018) ACS Catalysis, 8 (9), pp. 8058-8069. 

Manzoni, F., Wallerstein, J., Schrader, T.E., Ostermann, A., Coates, L., Akke, M., Blakeley, M.P., Oksanen, E., Logan, D.T. Elucidation of Hydrogen Bonding Patterns in Ligand-Free, Lactose- and Glycerol-Bound Galectin-3C by Neutron Crystallography to Guide Drug Design (2018) Journal of Medicinal Chemistry, 61 (10), pp. 4412-4420. 

Langan, P.S., Vandavasi, V.G., Cooper, S.J., Weiss, K.L., Ginell, S.L., Parks, J.M., Coates, L. Substrate Binding Induces Conformational Changes in a Class A β-lactamase That Prime It for Catalysis (2018) ACS Catalysis, 8 (3), pp. 2428-2437.