Lemke CT, Titolo S, Goudreau N, et al. A novel inhibitor-binding site on the HIV-1 capsid N-terminal domain leads to improved crystallization via compound-mediated dimerization. Acta Crystallogr D Biol Crystallogr. 2013;69(Pt 6):1115–1123.
Lemke CT, Titolo S, von Schwedler U et al. Distinct effects of two HIV-1 capsid assembly inhibitor families that bind the same site within the N-terminal domain of the viral CA protein. J Virol. 2012;86(12):6643–6655.
Lemke CT, Goudreau N, Zhao S et al. Combined X-ray, NMR, and kinetic analyses reveal uncommon binding characteristics of the hepatitis C virus NS3-NS4A protease inhibitor BI 201335. J Biol Chem. 2011;286(13):11434–11443.
Christopher Lemke, Ph.D.
Christopher Lemke is senior group leader of the Protein Science and Structural Biology group in the Center for the Development of Therapeutics (CDoT) at the Broad Institute of MIT and Harvard. He is in charge of the macromolecular X-ray crystallography and computational chemistry efforts of CDoT. His group enables and supports fragment-based screening and rational design of ligands for numerous discovery projects, which range from highly validated but so-called “undruggable” targets to exciting new targets identified through the Broad Institute’s genetics-based screening capabilities. His continuing goal and passion is the integration of structural biology, computational chemistry, and medicinal chemistry in the creation of innovative new treatments for human disease.
Before joining the Broad Institute in January 2014, Lemke worked for 10 years with Boehringer Ingelheim conducting structural studies of antiviral drug targets.
Lemke earned his Ph.D. from the University of Toronto in structural biology and biochemistry and holds a B.Sc. in applied biochemistry and genetics from the University of Guelph (Canada). His postdoctoral work was undertaken in the lab of Albert Berghuis at McGill University.
Contact Christopher Lemke at firstname.lastname@example.org.