Characterization of new crystallization chaperones
Exploring 3D structures of proteins facilitates deeper understanding of protein action and function by exploring the background of interaction patterns, effects of mutations and catalysis. The majority of structures are solved using protein crystallography: structure analysis by X-ray diffraction. The bottleneck of this method is preparation of crystallisable protein forms and single crystals for the measurements. A possible solution for crystallisation problems is enhancing crystallisation propensity by forming interactions favouring crystal formation: 1) by modifying protein surface or 2) using crystallization chaperons. The latter are proteins or protein modules of high crystallization propensity, bound to the target protein in a specific complex or as a fusion protein. The aim of this project is to construct and characterize new crystallization chaperone systems. New chaperons based on both protein/protein interaction and protein fusion will be created, and systematic analysis is planned to compare their effect on the crystallization propensities of various target proteins. Different crystal forms, diffraction quality and predictability of crystal contacts will be analysed as well, aiming improvement of our chaperon systems and developing crystallization chaperones for a wider range of target proteins.
Veronika Harmat, László Nyitray