From art to science in protein crystallography by LB nanotechnology

International Conference on Applied Crystallography

October 17-19, 2016 Houston, USA

Eugenia Pechkova and Claudio Nicolini

Genova University, Italy

Posters & Accepted Abstracts: J Material Sci Eng

Abstract :

Protein X-ray crystallography will remain the most powerful method to obtain the protein 3D atomic structures in foreseeable future. An impressive progress has been done in the last decades both in terms of instrumentation (X-ray sources of new generation, robotic systems and automatization) and data collection strategy and data reduction software, program and packaging, which permits to collect the data and solve the structure in the fast and optimal way. However, the crystal itself remains still the challenge for crystallographers. It particularly concerns the big protein such as membrane protein and protein complexes. In the post-genomic era, the structural and functional proteomics come to the forefront and this requires the fast and routinely successful structure determination of the huge number of proteins of the various nature and families, as well as their complexes with ligands, drugs or other protein, in order to understand protein-protein interaction, lying in the base of our understanding of all life processes and the major challenges of the century- cancer and the degenerative diseases. The new generation of synchrotrons and microfocus beamlines, as well as X-ray free lasers could accelerate the resolution of new protein structures of high industrial, pharmaceutical and fundamental life science interest. The routine production of the protein crystal of high quality (order, intensity of diffraction and radiation stability) is therefore very important. We hereby present the method capable to produce high quality protein crystal based on the LB (Langmur-Blodgett) nanotechnology, applicable to the any protein (high molecular weight and membrane proteins). In comparison to the standard crystallization protocols, the obtained crystals are more ordered and radiation stable. The process can be controlled AFM, QCM and by micro- and nano GISAX, giving the insight to the described phenomena which lead to trigger and accelerate protein crystallization by LB nano template. Moreover, highly ordered LB protein templates approach has the potential to solve the crystallization problem, also with the recent progress in X-ray free electron lasers.

Biography :

Email: eugenia.pechkova@gmail.com