Emmanuel Saridakis obtained a BSc in Physics (1991) and a PhD in Biophysics/ Crystallography (1995, supervised by Prof. D.M. Blow, FRS), both from the Physics Department, Imperial College London. He also holds an MSc in the History and Philosophy of Science (2000) from the LSE/ University of London.

After a series of post-doctoral research positions at the Biology Department of the University of Athens, the Physics Department and the Faculty of Medicine at Imperial College London and the Institute of Molecular Biology and Biotechnology/FoRTH in Crete, as well as teaching positions at the Technological Educational Institute (TEI) of Athens, he joined the Institute of Physical Chemistry at NCSR “Demokritos” where he was elected Researcher D in 2008 and Researcher C in 2013.

He is since 2018 a Senior Researcher (B) at the Laboratory of Structural and Supramolecular Chemistry of the Institute of Nanoscience and Nanotechnology of “Demokritos”, where he is in charge of the Laboratory of Macromolecular Crystallography, and a Honorary Senior Research Fellow at the Imperial College Faculty of Medicine (Protein Crystallisation Laboratory, headed by Prof. N.Ε. Chayen). He also spent one sabbatical year (2017) at the Centre de Biophysique Moléculaire/ CNRS-Orléans as a Le Studium/ Marie Sklodowska-Curie Fellow, working on the Rho transcription termination factor of M.tuberculosis. His main research interests are in the theory and methodology of macromolecular crystallisation and in X-ray crystallography of biological macromolecules of medical interest (but also smaller chemical structures).

E. Saridakis has pioneered the use of phase diagrams and various techniques for controlling crystal nucleation as a way both to optimise protein crystals for X-ray crystallographic structure determination and to discover new crystallisation conditions. Together with Prof. Naomi Chayen (Imperial College London), he developed various kinds of heterogeneous nucleation-inducing substances such as a specially designed type of Bioglass as well as protein-imprinted Molecularly Imprinted Polymers (MIPs). Together with Professors R. Sears (Surrey University) and Chr. Nanev (Bulgarian Academy of Science) he helped develop and apply theoretical aspects of protein crystal nucleation in the presence of such substances.

E. Saridakis has also played a major role in solving the X-ray crystallographic structures of a bacterial ferredoxin, various extracellular domains (and variants) of the bacterial disulphide bond protein DsbD, the human endoplasmic reticulum aminopeptidase ERAP2 on its own as well as complexed with various inhibitors (drug candidates), and the human insulin-regulated aminopeptidase IRAP complexed with various substrate analogues/ inhibitors. More recently, he participated in determining the X-ray crystallographic structure of a complex of the anti-HIV antibody RoAb13 with an epitope of CCR5, the receptor that plays a key role for the entry of HIV into cells, as well as in determining the cryo-EM structure of the RNA transcription termination factor Rho from Mycobacterium tuberculosis. All the above proteins and complexes are of wide medical and biological interest.

E. Saridakis has been for several years a member of the board of the International Organisation of Biological Crystallisation and of the Hellenic Crystallographic Association.

He has co-authored 49 publications in international peer-reviewed journals, one book chapter and two non-specialist books. He has presented his work at more than 40 international and national scientific conferences and workshops, in several of which as an invited speaker. His publications have been cited ca. 2890 times and his h-index is 27 (Google Scholar, January 2022).