RAMP is a network of 8 European universities plus the European Spallation Source, that is training 12 PhD students (ESRs in EU jargon), from 2017 to 2020. There are also 6 partner organisations.
It is coordinated from Université Grenoble Alpes by the consortium chair Prof Monika Budayova-Spano (Université Grenoble Alpes). The deputy chair is Prof Adrian Goldman (University of Leeds). The consortium website webmaster is Dr Richard Sear (University of Surrey).
The network members who are supervising the PhD students (ESRs) are:
- Prof Martin Caffrey (Trinity College Dublin, Ireland), a membrane structural and functional biologist. He studies membrane proteins involved in lipid metabolism, transport and signalling, using X-ray Scattering and Macromolecular crystallography, as well as biochemical and biophysical Methods.
- Prof Arwen Pearson (Universität Hamburg, Germany), a biochemist and protein crystallographer, working in a Physics department, leading a team including physical chemists, synthetic chemists, molecular biologists and physicists. We work on developing methods to probe protein dynamics and molecular mechanisms. Research in my group includes the development of new photochemical reaction initiation tools and sample delivery methods for time-resolved structural measurements, the development of improved X-ray data collection and analysis methods – including ways to mitigate radiation damage and the combination of X-ray data collection with complementary spectroscopic data. We apply all of this to understanding basic questions about the molecular mechanisms of membrane transporters, enzymes and viral assembly. For this project we’re working closely with Prof Henning Tidow, a specialist in membrane protein structural biology who works on membrane proteins involved in cell signalling and transport.
- Prof Bernadette Byrne (Imperial College London, UK) studies molecular membrane biology. Her research focuses on the structural and functional studies of eukaryotic transporters with particular emphasis on examples from fungi and plants, eg UapA from Aspergillus nidulans and Bor3 from Oryza sativa. We engineer proteins to make them more amenable to large scale expression, purification and structure determination by X-ray crystallography.
- Dr Richard Sear (University of Surrey, UK) is a computational physicist with extensive experience studying crystallisation. He is interested in understanding how crystals nucleate and grow, and why some conditions result in huge well-ordered crystals, while in other cases, we only observe poorly ordered crystals around 10 molecules across. Techniques used include computer simulation, simple theories, and experiment.
- Dr Jennifer McManus (Maynooth University, Ireland) is a physical chemist, leading the Soft Matter and Biophysical Chemistry research group in the University’s chemistry department. We use an interdisciplinary approach to understand how and why proteins assemble into ordered structures, such as crystals and fibrils or disordered amorphous aggregates, employing techniques from molecular biology, biochemistry, physical chemistry and physics.
- Dr Monika Budayova-Spano (Université Grenoble Alpes) has research interests centred on instrumental and methodological developments in the field of macromolecular crystal growth and crystallography. She also uses neutrons (as opposed to the more common X-rays) for structural studies addressing questions of broad biological significance concerning enzymatic mechanisms, ligand binding interactions, solvent effects, and structural dynamics. The instrumental and methodological developments cover controlling and monitoring the crystallisation process (nucleation and crystal growth) of biological macromolecules (crystal size, number and morphology). These are applied to structure determination approaches, such as crystallisation optimisation based on phase diagram investigation, and in situ methods for X-ray and neutron crystallography (including microfluidics). She is part of the Synchrotron Group at the Institut de Biologie Structurale in Grenoble.
- Prof Poul Nissen (Aarhus University) studies the structure and function of membrane transporters in particular cation pumps and lipid flippases of the P-type ATPase family and amino acid and neurotransmitter transporters (the SLC6 family). The laboratory uses a wide range of methods such as protein crystallography, small-angle scattering and electron microscopy and integrates structural studies, biochemistry and biophysics in a general theme of molecular neuroscience within the Nordic-EMBL Partnership for Molecular Medicine. Projects of RAMP will focus on rational approaches for membrane protein crystallization using lipid-based methods in particular.
- Dr. Esko Oksanen (European Spallation Source) is a protein crystallographer developing instrumentation for neutron protein crystallography and is responsible for a project to build a macromolecular diffractometer at the ESS, which will be the world’s brightest neutron source. His research interests involve the role of hydrogen atoms in enzyme mechanisms, drug binding and bioenergetics.
Professor Adrian Goldman (University of Leeds), is a structural biologist, and holds the Chair in Membrane Biology in Leeds’ School of Biomedical Sciences. His research focuses on understanding interactions in or near the membrane, including the protein/sodium pumping pyrophosphatases that occur in protozoan parasites, membrane transporters and cell signalling in tyrosine kinase receptors. Our primary technique is diffraction, using x-ray crystallography, electron microscopy and in the future neutron crystallography.
The network also has partners:
- MiteGen (Ithaca, NY, USA) MiTeGen engineers, manufactures and distributes a full range of the leading products for the crystallisation, crystal harvesting, cryocooling and X-ray diffraction data collection. MiTeGen has partnered with leaders in the membrane protein research community to co-develop and commercialise novel platforms that enable new methods and techniques for use in further understanding of membrane protein structure and function. MiteGen customers include academic, medical, pharmaceutical, government and industrial laboratories in more than 45 countries. MiteGen was founded in 2004.
- Molecular Dimensions (Newmarket, Suffolk, UK) is a world leading supplier of modern screens, reagents, other consumables and instrumentation for protein structure determination by X-ray crystallography. Headquartered in Newmarket (UK) it has offices in the USA and distribution in Asia.
Founded in 1998 to provide specialist products for crystallographers across the world, it has grown through alliances with leading scientists aimed at developing and commercialising innovative ideas.
- NatX-ray (Grenoble, France) is a major player in the field of X‑ray crystallography, designing, manufacturing and selling its exclusive innovative G-Rob™ system, a solution for sample and equipment handling, as well as automated data collection. The G-Rob™ technology is now widely in use at various synchrotron beamlines and on neutron sources around the world. NatX-ray also provides a full line of benchtop equipment such as UV microscopes, crystallization bench and micro-spectrophotometers, and distributes proprietary consumable products such as phasing kits and compounds, as well as a full range of popular brands of crystallography products for laboratories and synchrotrons. NatX-ray has a subsidiary in San Diego, California, USA.
- Novartis is a global healthcare leader and has one of the most exciting product pipelines in the industry today. The protein science group in the Chemical Biology and Therapeutics (CBT), Novartis Institutes for Biomedical Research (NIBR), Basel is at the interface of biology and chemistry. We deliver structural information on target proteins and their interactions with ligands to guide and support integrated lead finding and optimization. Our yearly portfolio includes more than 40 pharmacologically relevant targets including several classes of integral membrane proteins (IMP). We have a structural biology platform for IMP, including parallel expression and purification, antibody production for complexes, biophysical characterization and structural biology (X-ray crystallography and electron microscopy).
This webpage is work in progress …