Dr. John Vakonakis obtained his BSc in Biology from the University of Crete (Greece) in 1999 before moving to Texas A&M University (USA) where he did his PhD in Biochemistry. In 2005 he moved to Oxford for postdoctoral research on Structural Biology. Between 2007 and 2009 he was Marie Curie Fellow and Junior Research Fellow at Trinity College, Oxford. Following a brief stint as beamline researcher at the Swiss Light Source, John established his independent research group at the Department of Biochemistry supported by the Wellcome Trust. He was appointed Associate Professor in Structural Biology and Biophysics and Fellow of Lincoln College in 2013. He also serves as a college Harassment Advisor and the Website Fellow.
John teaches Biophysical Methods for the undergraduate degree in Biochemistry and supervises the Protein Purification practical laboratories. He also accepts students from the Biochemistry, Chemistry and Pharmacology MSc courses who wish to do their research degree on structural biology. At Lincoln, John primarily tutors students on Biological Chemistry, Biophysics, Structural Biology and Data Analysis.
John’s research focuses on understanding the mechanistic links between large-scale molecular assemblies in cells and their function. Recent topics include the processes by which cell organelles are formed and how malaria parasites re-engineer human red blood cells. His group specializes in integrating multiple biophysical methods, including X-ray crystallography, NMR and electron microscopy, to tackle these questions. For details of current research projects please visit the group's departmental page.
Selected recent publications
1. Cutts EE, Laasch N, Reiter DM, Trenker R, Slater LM, Stansfeld PJ, Vakonakis I (2017) Structural analysis of P. falciparum KAHRP and PfEMP1 complexes with host erythrocyte spectrin suggests a model for cytoadherent knob protrusions. PLoS Pathog. 13, e1006552.
2. Rogala KB, Dynes NJ, Hatzopoulos GN, Yan J, Pong SK, Robinson CV, Deane CM, Gönczy P, Vakonakis I (2015) The Caenorhabditis elegans protein SAS-5 forms large oligomeric assemblies critical for centriole formation. eLife 4, e07410.
3. Oberli A, Slater LM, Cutts E, Brand F, Mundwiler-Pachlatko E, Rusch S, Masik MFG, Erat MC, Beck HP, Vakonakis I (2014) A Plasmodium falciparum PHIST protein binds the virulence factor PfEMP1 and comigrates to knobs on the host cell surface. FASEB J 28, 4420-4433.
4. Hilbert M, Erat MC, Hachet V, Guichard P, Blank ID, Flückiger I, Slater L, Lowe ED, Hatzopoulos GN, Steinmetz MO, Gönczy P, Vakonakis I (2013) The Caenorhabditis elegans centriolar protein SAS-6 can form a spiral that is consistent with imparting a 9-fold symmetry. Proc. Natl. Acad. Sci. U.S.A. 110, 11373-8.
5. Kitagawa D, Vakonakis I, Olieric N, Hilbert M, Keller D, Olieric V, Bortfeld M, Erat MC, Flückiger I, Gönczy P, Steinmetz MO (2011) Structural Basis of the 9-Fold Symmetry of Centrioles. Cell 144, 364-75.