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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.
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.
Neutrons have shown how massive enzyme complexes inside cells might determine whether sugar is burnt for energy or stored as fat. These findings will improve understanding of diabetes and a range of metabolic diseases.
Scientists using neutrons at the Institut Laue-Langevin (ILL) have shown how pyruvate dehydrogenase complexes (PDCs) could control the rate of sugar metabolism by actively changing their own composition. The research is published in the Biochemical Journal.
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.
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.
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.
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.