Acquisition of automated platforms for the analysis and photodocumentation of crystallization assays of biological macromolecules and high-performance scanning of bioactive compounds

• Grant number: 09/54077-9
• Support Opportunities: Multi-user Equipment Program
• Start date: August 01, 2010
• End date: July 31, 2012
• Field of knowledge: Biological Sciences - Biophysics - Molecular Biophysics
• Principal Investigator: Iris Concepcion Linares de Torriani
• Grantee: Iris Concepcion Linares de Torriani
• Host Institution: Centro Nacional de Pesquisa em Energia e Materiais (CNPEM). Campinas , SP, Brazil
• City of the host institution: Campinas
• EMU web page: Página do Equipamento Multiusuário não informada
• Type of equipment: Tipo de Equipamento Multiusuário não informado
• Manufacturer: Fabricante não informado
• Model: Modelo não informado

Abstract

The principal objective of this project is to obtain the complementary instrumentation needed in order to achieve full automation and efficiency in the field of crystallization and in the performance of bioassays of biological macromolecules. The Center for Molecular and Structural Biology is equipped with all of the infrastructure necessary for cloning, expressing, and purifying proteins, as well as for developing crystallization assays, this last being partially automated. The full automation and miniaturization of the crystallization process will allow thousands of conditions for the growth of crystals to be tested in a rapid and efficient manner. A system for the identification, photodocumentation, and remote analysis of crystals is indispensable for consolidating the substantial gains made (time saved) with automated crystallization. The National Synchrotron Light Laboratory has two beamlines dedicated to protein crystallography. This places the Laboratory in a privileged position in Brazil and in South America, allowing competitive, world-class experiments to be conducted. With the synchrotron light source instrumentation that is currently on the market, a wiggler beamline in particular, we would be able to achieve even greater resolution of the structures of biological macromolecules. The crystallization process is recognized as a true stumbling block to advances in molecular and structural biology, and it is therefore essential to focus our efforts on overcoming this obstacle. The possibility of performing in situ assays is also of great importance for research into the interactions between proteins and inhibitors, which could lead to applications for the identification of bioactive compounds. Consequently, this proposal is aimed at the acquisition of a system of analysis and documentation of protein crystals that allows the visualization and photodocumentation of the assays. A plate reader that allows the large-scale automated scanning of bioactive compounds would complement this equipment, allowing the production of samples to reach a level in keeping with the methods of structural analysis available in the laboratory. (AU)