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Monika Budayova-Spano
Associate Professor
Faculty of Pharmacy, University Grenoble Alpes (UGA)
Synchrotron Group (GSY), Institut de Biologie Structurale (IBS)
CEA-CNRS-UGA UMR 5075
71, Avenue des Martyrs, CS 10090, 38044 Grenoble cedex 9, France
Tel: + 33 4 57 42 85 64
Email: monika.spano@ibs.fr
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I have been educated as a physicist (biophysics and chemical physics at the University Comenius Bratislava Czechoslovakia, protein engineering & genome sequencing and material science at the University Aix-Marseille II France). After a PhD thesis devoted to crystallization and characterization of proteins in solution studying the phase diagrams, growth kinetics and molecular associations (1994-1998) at the CRMC2 Marseille, a brief postdoctoral position at the ICSN Gif sur Yvette in protein purification, a second postdoctoral position at the IBS Grenoble in X-ray protein crystallography and a third postdoctoral position at the European Molecular Biology Laboratory (EMBL) Grenoble in neutron protein crystallography, in September 2006 I finally entered University Joseph Fourier (Université Grenoble Alpes) in Grenoble. I am Associate Professor at the Faculty of Pharmacy. I have organized, taught and co-taught different courses, tutorials and practical on subjects ranging from physics, biophysics, mathematics, informatics and (biological) crystallization. To date I have supervised 1 Master degree (April – August 2006), 2 Bachelor’s degree (January – February 2011 and June – July 2012), 2 PhD students (September 2007 – September 2008 and November 2013 – November 2016) and 1 Postdoc researcher (February 2010 – September 2011). My research interests are centered on the diverse instrumental and methodological developments in the field of macromolecular crystal growth and crystallography as well as on the (neutron) structural studies addressing questions of broad biological significance concerning enzymatic mechanism, ligand binding interactions, solvent effects, structure dynamics and their implications. The instrumental and methodological developments cover controlling and monitoring the crystallization process (nucleation and crystal growth) of biological macromolecules (crystal size, number and morphology) for different downstream structure determination approaches, crystallization optimization based on phase diagram investigation, and development of novel tools and approaches to protein crystallization regarding in situ methods for X-ray and neutron crystallography (including microfluidics). I was scientific co-responsible of Laue Diffractometer dedicated to neutron protein crystallography at the ILL (April 2008 – April 2009). Therefore I has tutored PhD students and PostDocs coming from inside as well as outside EMBL/ILL in optimizing crystals or in performing the neutron diffraction experiment. I attend regularly the International Schools on Biological Crystallization, in Granada Spain sponsored by IUCr, and in Nové Hrady Czech Republic sponsored by FEBS, where I am invited to give lectures and tutorials on large crystal growth for neutron protein crystallography. Currently, I am developing my research activities within the Synchrotron Group at the IBS. I am responsible for a new crystallization platform called OptiCrys, dedicated to X-ray as well as neutron protein crystallography, available under a collaborative mode on French beamline for Investigation of Proteins BM30A at the ESRF (http://www.fip-bm30a.fr/index.php/trading-hours-and-holidays/manage-diaries/description/10-services-available-on-fip). OptiCrys is a crystal growth apparatus for Optimization of protein Crystallization. It consists in a novel fluidic system incorporated into the crystal growth bench that, in addition to accurate temperature control (with a temperature range of 233K-353K), also allows chemical composition of the crystallization solution (e.g. precipitant concentration, pH, additive) to be varied in an automated manner. OptiCrys enables monitoring and controlling the crystallization processes that allow producing crystals of specific sizes and morphology optimized for different downstream structure determination approaches. I am involved in several national and international collaborations.