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RAtionalising Membrane Protein crystallisation

Project description

Microfluidics-based method for membrane protein crystallisation

Determining the 3D structure of membrane proteins from exploitable crystal samples represents a significant technical challenge, given the complexity and instability of these biological macromolecules. Despite their importance as drug targets, only 600 unique membrane protein crystal structures have been determined to date. Consequently, there is an imminent need to develop reliable methods for crystallising membrane proteins. Funded by the Marie Skłodowska-Curie Actions programme, the RAMP project proposes to incorporate microfluidics-based technology in the crystallisation process for precise control of experimental conditions and the properties of the crystals generated. By focusing on membrane transporters, the researchers hope to provide unprecedented insights into the function of target proteins and pave the way for relative drug design.

Objective

Membrane proteins form more than 85% of drug targets, but just 600 unique membrane protein crystal structures have been determined. A better understanding of how to crystallize membrane proteins reliably is therefore urgently required. The Innovative Training Network “RAtionalising Membrane Protein crystallisation” – RAMP will bring together cutting-edge physical chemistry methods for crystallisation condition control and phase diagram exploration, and the development of new lipids and screens in conjunction with industry with the most challenging biological problems. The network includes expert academic and industrial research groups in crystallisation theory, methods development, membrane protein crystallography, drug development and novel structural techniques like time-resolved and neutron crystallography. We will develop new, rational methods for crystallising membrane proteins, focusing particularly on transporters that are also interesting drug targets. The new robust crystallisation methods will also allow us to use emerging European research infrastructures like XFEL or ESS to gain insight into membrane protein function because the techniques will provide the necessary precise control of crystal size.
A structured training programme organized by academia and industry together will equip the early stage researchers with the skills needed for a successful research career in the field of structural biology. Frequent secondments, research visits and meetings between early-career scientists ensure an efficient exchange of ideas and practical experiences between different groups leading to better integration of European research and innovations in structural biology. Supervision and mentoring by several senior scientists will give the researchers a strong scientific education and make them highly competitive in the work place of tomorrow. The work programme here will improve European competitiveness and advance graduate training.

Coordinator

UNIVERSITE GRENOBLE ALPES
Net EU contribution
€ 525 751,20
Address
621 AVENUE CENTRALE
38058 Grenoble
France

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Region
Auvergne-Rhône-Alpes Rhône-Alpes Isère
Activity type
Higher or Secondary Education Establishments
Links
Total cost
€ 525 751,20

Participants (9)