“SEE-STRUCT” is structure-oriented module of SEE-DRUG project and aims to the structural elucidation of proteins, enzymes and other interesting drug-targets. The tools offered for these efforts are a state-of-the-art high field NMR instrument of 700 MHz equipped with a highly sensitive probe and crystallization robot.

SEE-STRUCT: Conformational dynamics, interactions & biophysical characterization, to provide atomic-level insight on individual proteins and protein-protein/drug candidates interaction, to identify new protein-protein interactions and to investigate the physicochemical properties (dynamics, affinity, kinetics, etc) of these interactions, based on NMR methods, automated crystallization, crystal structure determination and other complementary techniques. Additionally, NMR is a well-established key technology at the forefront of structural biology and is a particularly versatile tool. NMR analysis is equally valuable in elucidating dynamical properties of individual or interacting biomolecules that can be further tested through complementary tools, such as cell-based assays. In addition, NMR can distinguish and characterize primary or secondary interaction sites, determine the binding affinity of substrates, monitor changes in the conformation or the dynamic properties and overall contribute to the structure-based functional characterization of biomolecules. Moreover, NMR is also applied to monitor the thermodynamic along with the kinetic parameters of protein-protein interaction, an understanding that is crucial in going up a level in comprehending complex interactions in a systems biology context. The installation of the 700 MHz NMR instrument, suitable for proteins >20 kDa and equipped with a cryogenically cooled probe through SEE-DRUG will provide unprecedented possibilities to Greek academic/research staff and industrial stakeholders, such as: (a) in-depth, atomic-level insight into the structure, (b) high resolution and sensitivity for analysis of a variety of fluids (food, olive oil, wine, biofluids, etc.), (c) fast acquisition, allowing real-time NMR use to monitor dynamic processes, and (d) high-throughput structure determination. A crystallization robot will be strongly coupled with the NMR facility. Initial screening of protein-targets with NMR (to confirm, folding, oligomerization state, solubility etc.) will be followed by crystallization screening conditions in order to produce protein-substrate/drug complexes. The coupling of the two instruments will be time and cost-efective since it will reduce the faulse attempts to crystallize structureless or self-aggregating proteins.