An international team of researchers from IBS and ILL, among others, has shed light on the molecular mechanism behind the importance of water for functional protein dynamics. The scientists have discovered that water’s ability to flow on the surface of proteins makes them sufficiently dynamic to be biologically active. The results have just been published in Nature Communication.
An EPN campus success story! [More on the ILL website]
Merci aux centaines de visiteurs qui ont visité notre chapiteau et arpenté le site de recherche EPN, le samedi 18 octobre.
A la demande générale voici les résultats du jeu-quiz sur le thème de la cristallographie (les questions puis les réponses pages 5 et 6). Les gagnants seront avertis dans les prochains jours.
In soft matter and materials physics, self-assembly serves to synthesize and control nano-structures with well-defined sizes and geometries. Accurate control of the properties (structure and dynamics) of these nanoparticles is essential for the performance relevant to a wide range of products. A new mechanism has just been observed due to the unique combination of the high resolution of synchrotron SAXS combined with the contrast of SANS. An EPN success story! See more on ILL website.
The epn campus site entrance is now located at 71 avenue des Martyrs, Grenoble. It is not possible anymore to access the site via the former site entrance on rue Horowitz.
Please see here how to travel to the EPN science campus.
Friday 21 February saw the official opening on the epn campus of several new buildings which were funded in part or in full by the local and regional authorities in the framework of a so-called CPER contract (Contrat de Projets Etat-Région). The opening ceremonies were attended by the French Minister for Higher Education and Research, Geneviève Fioraso, the President of the Rhône-Alpes region, Jean-Jack Queyranne, the President of Grenoble Alpes Metropole, Marc Baïetto, and deputy Mayor of Grenoble, Jérôme Safar, in their capacity as funders and faithful supporters of these projects. [more on the ILL website]
With the arrival of 240 IBS specialists on the site, the epn campus reaffirms the international level of its research capacities in structural biology.
Building ribosomes – the cell’s protein factories – is like a strictly choreographed dance. Other ‘machines’ inside the cell have to produce specific RNA molecules and fold them into the right shape, then combine the folded RNA with proteins to form a working ribosome. The study combined nuclear magnetic resonance experiments performed at EMBL and neutron scattering experiments performed at the ILL in Grenoble, France.
Neutron scattering at ILL and ISIS delves inside new crime scene forensics technique developed by the University of LeicesterResearch to address the fact that only 10% of fingerprints taken from crime scenes yield identifications that are usable in court
Harvesting unused energy has been the object of research since the days of the windmill and the waterwheel. In recent years, thermo-electric materials have enabled the re-use of otherwise wasted thermal energy as electrical power. Driven by the quest to efficiently cool densely packed micro-electronics chips, they are also used as solid-state refrigerators. One of the difficulties involved in developing thermo-electric systems that convert heat into electric current is the need for materials exhibiting high electrical conductivity but low thermal conductivity, which is only possible with complicated crystal structures. Scientists have now discovered a way of suppressing thermal conductivity in sodium cobaltate, opening new paths for energy scavenging.
Metals contained in nanoparticles can enter into the food chain. Scientists have, for the first time, traced the nanoparticles taken up from the soil by crop plants and analysed the chemical states of their metallic elements. Zinc was shown to dissolve and accumulate throughout the plants, whereas the element cerium did not dissolve into plant tissue. The results contribute to the controversial debate on plant toxicity of nanoparticles and whether engineered nanoparticles can enter into the food chain.
Developments arising from new science techniques at Keele University in the UK, the ILL and the ESRF have confirmed the presence of hydronium ions in the protein rubredoxin. The study provided a major advance well beyond anything achieved previously, and has opened up a new and extremely important area of protein science.
Synchrotron X-rays confirm a new method for X-ray image processing.
Scientists have developed a way to produce three-dimensional X-ray images of the breast at a radiation dose that is lower than the 2D radiography methods used in clinics today. The new method enables the production of 3D diagnostic computed tomography (CT) images with a spatial resolution 2-3 times higher than present hospital scanners, but with a radiation dose that is about 25 times lower.
Understanding will help protein’s potential application in biochemical gas sensors or in state-of-the-art wound dressing.
A team of ILL users dissolved iron in liquid surfactant to create a soap that can be controlled by magnets. The discovery, published today in Angewandte Chemie, could be used to create cleaning products that can be removed after application and used in the recovery of oil spills at sea.
ILL just implemented a new policy to to better define, manage and exploit the scientific data collected there. See more information and the complete document on the ILL website.
The new ILL data policy will be applied from 2012 onwards, starting with those proposals accepted at the next proposal round (deadline 15 February 2012).
The CRISP Project is bringing together eleven main players from across Europe to address four key technology areas for the big science of tomorrow, among which ESRF and ILL. CRISP was launched on 17 October at the Czech Embassy in Paris.
How do we bridge the gap between cutting-edge research and the science lessons taught in schools? How to instil a taste for science into today’s youngsters? Is it possible to inspire them through the international and multidisciplinary atmosphere reigning in world-class research institutes such as the ESRF, ILL and EMBL? During four days, from 9 to 12 October, the labs, meeting rooms and corridors of the EPN Science Campus resonated with activity of teachers aiming to answer questions such as these.
Under the umbrella of the large-scale facilities technology platform (PT-G), the EPN institutes attended the Rendez-vous Carnot which took place in Lyon on 12&13 October.
'Les Rendez-Vous CARNOT' is one of the largest gatherings of research laboratories in Europe. It brings together players in research and in industry.
Through many interviews, the TP-G partners gave a comprehensive view of the scope of the applied research that will be available through the TP-G, as well as its value.
Congratulations to Daniel Shechtman on the award of his Nobel Prize for Chemistry! Shechtman's discovery of quasicrystals was an extremely important step in fundamental solid-state chemistry and physics, and it has changed the way we see crystals and long range order.
There has been substantial related work done in this area both with neutrons at the ILL and with x-rays at the ESRF. Marc de Boissieu, a CNRS researcher at SIMAP (CNRS/Grenoble INP/ UJF), has been leading for more than 20 years now cutting-edge experiments on the structure and dynamics of quasi-crystals. “Although progress has been made, much remains to be done to understand fascinating quasicrystals and the related complex metallic alloys”, says de Boissieu.
Neutrons have shown the movement of cholesterol between and within cells takes far longer than previously thought. Findings could impact the treatment of a range of diseases linked to abnormal rates of cholesterol transfer.
Scientists have discovered a feeding mechanism for the conodont, an extinct sea creature resembling an eel but perhaps a closer relation to today's lampreys. Their study may have implications for our understanding of the evolution of the first vertebrates.
ILL neutrons have proved the viability of a new radioisotope for better targeted cancer therapy. Terbium 161 has ideal properties for targeting cancerous cells whilst minimising damage to surrounding healthy tissue. A new paper published in Nuclear Medicine and Biology has described a method for producing sufficient quantity and quality of Tb161 to treat hundreds of patients a week!
An international group of scientists from Italy, the UK and France used a powerful new synchrotron X-ray technique to observe for the first time at the molecular scale how muscle proteins change form and structure inside an intact and contracting muscle cell.
The ILL, ESRF, CEA and CNRS are seeking to extend their research expertise and exceptional technological facilities to industrial users. To this end, on 16 February the institutes signed an agreement for the creation of a technology platform on the GIANT site dedicated to the characterisation of materials and processes, a crucial and inevitable step forward for tomorrow's technologies.
One of the latest generation of electron microscopes was inaugurated at the IBS on February 11 in presence of the funding bodies and Guillaume Lissy, representing the President of the Rhône-Alpes Region.
This FEI Tecnai Polara microscope, the second of its kind in France, will allow scientists to:
- visualize biological macromolecular complexes at the nano or pseudo-atomic scale and determine their three-dimensional structure
A mini-symposium by experts of cryomicroscopy and tomography concluded this event. This microscope is unique in the south of France.
Good news for Grenoble! The "Institut de Recherche Technologique (IRT) NanoElectronique" project is one of the six national projects selected by the French government for funding within the IRT programme in the Grand Emprunt scheme. ESRF and ILL’s characterisation Technology Platform will be a direct beneficiary.
On 26th September 2011, the European Spallation Source and the Institut Laue-Langevin initiated an extensive collaboration for research and development activities within neutron science. In a Memorandum of Understanding, ILL and ESS set the framework for the future cooperation, which aims at developing joint scientific and technological projects.
A collaborative effort between scientists at the ILL, Los Alamos National Laboratory, Keele University, ISIS, and the University of Toledo has resulted in the remarkable observation of hydroxonium ions that are thought to be involved in proton transfer during enzyme-catalysed reactions.
The work, which used ILL's D19 diffractometer, exploits the remarkable ability of neutron diffraction to visualise hydrogen atoms and therefore to be able to distinguish between hydroxonium ions and water molecules - this is typically impossible using X-ray crystallography. The enzyme studied was xylose isomerase - this is an enzyme of high biological and biotechnological significance, and one where changes in the location of hydrogen atoms are crucial to catalytic activity that is associated with converting D-xylose to D-xylulose. It turns out that hydroxonium ions replace metal ions and may be involved in the templating specific sites for the binding of metal ions. The work explains how the activity of the enzyme decreases dramatically at low pH.
New biophysics data collected at ILL and ESRF will help biochemists make in vitro experiments more physiologically relevant by taking into account macromolecular "crowding" inside cells.
Researchers found that crowding has a significant effect on protein diffusion at the nanosecond timescale. This has implications for all biochemical processes and reaction rates when comparing lab results to cell physiology.
Researchers of the IBS, in collaboration with their colleagues of the UVHCI and the AFMB, report the first in situ observation of the intrinsically disordered domain of the nucleoprotein of measles virus.
Using nuclear magnetic resonance spectroscopy, small angle scattering, and electron microscopy, they have obtained a structural characterization of the intrinsically disordered C-terminal domain of the nucleoprotein in the context of the entire N-RNA capsid. Their results, published online by PNAS, suggest that this intrinsically disordered part plays an important role in infection by measles virus.