Institut de Biologie StructuraleGrenoble / France

Press releases

Press Releases since 2015 can be found bellow:

2017 - 2016 - 2015


11/0917 - Ultra-fast molecular movie: watching proteins absorbing light
Using a revolutionary method, scientists have been able to film ultra-rapid processes at work in fluorescent proteins, which are extensively used as markers in in vivo imaging. This new method, which uses enormous X-ray lasers, permits the analysis of processes such as vision, bioluminescence and other phenomena which have not been observable to date. These results are to be published in Nature Chemistry on September, the 11th, as part of an international collaboration involving scientists from the IBS, the Universities of Lille, Rennes 1 and Paris-Sud, and the Max Planck Institute for Medical Research at Heidelberg in Germany.
Press release

15/05/2017 - How plankton dominate ocean life
Photosynthesis is a unique process that allows independent colonization of the land by plants and of the oceans by phytoplankton. Although the photosynthesis process is well understood in plants, scientists are still unlocking the mechanisms evolved by phytoplankton to achieve extremely efficient photosynthesis. Researchers from the Institut de Biosciences et Biotechnologies de Grenoble (BIG), the Institut de biologie structurale (IBS), the Institut nanosciences et cryogénie (INAC), the Institut de Biologie Physico-Chimique (IBPC), ETH Zurich (Switzerland) and University of Konstanz (Germany), combine biochemical, structural and in vivo physiological studies to unravel the structure of the plastid in diatoms, prominent marine eukaryotes. The results of this study were published in Nature Communications on June 20, 2017.
Press release (in french only)

15/05/2017 - Insights into a mechanism which inhibits root cell elongation
The Methods and Electron Microscopy group in collaboration with the Laboratoire de Biologie végétale et microbiologie environnementales Cadarache and the Leibniz Institute of Plant Biochemistry have revealed a mechanism for plant root growth arrest during low phosphate availability in soil.
These results may improve crop plants resistance in acidic soil or depleted in phosphate, or increase their pollutant metal extraction properties. The results of this study were published in Nature Communications on May 15, 2017.
Press release (in french only)

25/04/2017 - Polyvalan (IBS & ENS Lyon Spin-off company) and Pulsalys sign an exclusive exploitation contract to easily determine the 3D structure of proteins
PULSALYS, the Lyon-Saint-Etienne Technology Transfer Acceleration Company, announces the signature of an exclusive license with POLYVALAN to facilitate the determination of protein structures. POLYVALAN, which benefits from the know-how of IBS and ENS-Lyon, specializes in the development, manufacture and marketing of innovative chemical additives dedicated to structural biology.
Press release


18/04/2016 - Binding to produce flowers
The LEAFY protein, a transcription factor responsible for flower development, is able
to assemble itself in small chains made up of several proteins. This mechanism allows it to bind to and activate regions of the genome that are inaccessible to a single protein. These results were obtained by scientists in the Laboratoire de Physiologie Cellulaire Végétale and the Institut de Biologie Structurale, working in collaboration with their international partners. Published on 21 April 2016 in Nature Communications, they open the way to new research opportunities regarding the regulation of gene expression.
Press release

17/05/16 - A progress in the search for an AIDS Vaccine
A sub-Saharan African donor’s blood has yielded remarkable finds that could be crucial in the search for an AIDS vaccine. An infected donor’s immune system naturally made potent antibodies, which lab tests showed could effectively recognize and neutralize about 50 percent of all HIV-1 strains circulating around the world. HIV-1 is the most widespread HIV type globally. Researchers managed to observe and understand the process of how the immune system developed these antibodies, which could advance vaccine design.Retour ligne automatique
This study undertaken by scientists from the International AIDS Vaccine Initiative, The Scripps Research Institute, the University of California San Diego, Monogram Biosciences Inc., Rwanda-Zambia HIV Research Group, Academia Sinica, the Ragon Institute of MGH, MIT, and Harvard, and the Institut de Biologie Structurale was published on May 17 in the journal Immunity
Press release

07/06/2016 - Kinetics and RNA sequence dependence of measles virus nucleocapsid
Measles virus RNA genomes are packaged into helical nucleocapsids (NCs), comprising thousands of nucleo-proteins (N) that bind the entire genome. N-RNA provides the template for replication and transcription by the viral polymerase and is a promising target for viral inhibition. The nucleocapsid assembly process regulating this process has been described for the first time by IBS researchers thanks to a combination of real-time NMR, fluorescence spectroscopy and electron microscopy. This observation is reported in Angewandte Chemie on June 06.
Press release-(in french only)

05/09/2016 - Scientists use neutrons to understand the secrets of extremophile bacteria like the ones decomposing the RMS Titanic
Understanding microbe adaptation to extreme environments remains a challenge of high biotechnological potential—in bioremediation and waste management, for example. Halomonas microorganisms isolated from the oceans or salt marshes, reversibly accumulate high concentrations of the molecule ectoine, within their cells, to counterbalance fluctuating external salt concentrations. It has been estimated that a rust- producing Halomonas species could bring about the total deterioration of the sunken RMS Titanic by 2030. A range of specialised neutron scattering experiments were designed in order to understand how ectoine permits Halomonas to survive in their extreme environment. They revealed that within the microbe cells, ectoine acts by enhancing the remarkable dynamic properties of water that are essential to life processes.
Press release

28/029/2017 - X-rays Reveal New Path In Battle Against Mosquito-borne Illness
Could we get rid of mosquitoes without polluting the environment? Yes, we can! The BinAB toxin, produced in crystal form by a bacterium, specifically kills the larvae of Culex and Anopheles mosquitoes, but it is inactive on tiger mosquitoes (or Aedes), the vectors for dengue fever and chikungunya. Knowledge of the molecular structure of BinAB is necessary if we are to broaden its spectrum of action. Having long been inaccessible, this structure is now being published on 28 September 2016 in Nature by an international consortium involving scientists from the IBS, UCLA, UCR and SLAC in the USA.
Press release


09/12/2015 - Large Scale Conformational Dynamics Control the Function of H5N1 Influenza Polymerase
An international collaboration of scientists from the IBS (FDP group), the EMBL and the ILL has revealed the molecular function of a protein essential for replication of H5N1 influenza virus. Scientists used a combination of solution-state NMR, small-angle neutron scattering, small-angle X-ray scattering (SAXS), and Förster resonance energy transfer (FRET) to reveal structural changes in the 627-NLS domain of the Influenza A RNA polymerase. This domain is able to adopt two very different conformations, adjustable according to the needs of the virus. Depending on the temperature, this protein assumes a ‘close state’, allowing the polymerase to run and the viral proteins to be synthesized, or an ‘open-form’ observed here for the first time, giving its ability to interact with other proteins and thus allowing entry in infected cell nucleus. Switching from one conformation to another enables an essential part of the polymerase to enter the nucleus of the infected cell, where the viral genome is replicated. This study illustrates how the conformational flexibility of a protein allows it to adapt its function, facilitating infection of the host.
Press release

08/10/2015 - New light on transit into and out of the nucleus of the cell
The essential mechanism by which molecules are transported into the nucleus of the cell has been revealed by an international collaboration implicating researchers at the Institut de Biologie Structurale (Grenoble), the EMBL (Heidelberg), the Heidelberg Insitute of Theoretical Studies, and the University of Cambridge. Combining in vitro and in vivo experimental observations and simulation, the consortium was able to demonstrate how nucleoporins, highly flexible proteins present in the pores of the nuclear envelope, create a selective barrier by exploiting multiple, weak interactions with the transporting proteins, allowing for rapid but selective passage into the nucleus.
Press release

05/10/2015 - Molecules can still move, even inside crystals
X-ray crystallography reveals the three-dimensional structure of a molecule, especially for therapeutic or biotechnological purposes. For the first time, a study has shown that residual movements continue to animate proteins inside a crystal and that this movement ’blurs’ the structures obtained via crystallography. The study stresses that the more these residual movements are restricted, the better the crystalline order.
Press release (in french only)

06/05/2015 - Versatile Switch for Light-Controlled Cells

Scientists from IBS, Jülich, Frankfurt and Moscow uncovered the atomic structure of KR2, a light-driven transporter for sodium ions which had only recently been discovered. Based on the structural information the team then identified a simple way to turn KR2 from a sodium- into a potassium pump using simple means.
Integrated into neurons, this could make KR2 a valuable tool for optogenetics, a new field of research that uses light-sensitive proteins as molecular switches to precisely control the activity of neurons and other electrically excitable cells using light impulses.
Press release

30/04/2015 - Direct observation of hierarchical protein dynamics
Proteins are complex machines that are in constant motion, moving continuously in order to carry out their functions. Their multiple component atoms also have their individual motion patterns, making the entire protein a system of non-stop highly complex movement. Understanding how a protein moves is the key to developing drugs that can efficiently interact with it. But because of its complexity, protein motion has been notoriously difficult to study. Scientists at IBS-Grenoble, EPFL and ENS-Lyon, have developed a new method for studying protein motion by first freezing proteins and then slowly “waking them up” with increasing temperature.
Press release

27/04/2015 - Alzheimer’s disease markers could be identified through protein water mobility
A study of the water mobility on the surface of tau protein fibres has been conducted by a global team of scientists using neutron scattering experiments at the Institut Laue-Langevin (ILL) in Grenoble, France and the Jülich Centre for Neutron Science at the Heinz Maier-Leibnitz-Zentrum (MLZ) in Garching, Germany. The IBS scientists (from the Dynamics and kinetics of molecular processes Group) found water mobility on the surface of tau protein fibres is increased; the findings suggest that the movement of water molecules could be a marker for the presence of amyloid tau fibres and contribute to the detection of Alzheimer’s disease.
Press release

16/04/2015 - How water molecules dance to activate proteins
An international team of researchers from the IBS (DYNAMOP group), the Institut Laue-Langevin, the Forschungszentrum Jülich, the University of California Irvine, the Australian Institute of Science and Technology Organisation, the Max Planck Institute Mülheim and the University of Perugia 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.
Press release

29/01/2015 - Visualizing the Molecular Recognition Trajectory of an Intrinsically Disordered Protein
For the first time, IBS researchers observed at atomic scale the trajectory and successive changes of shape of a viral disordered protein, from its free state to its attachment to another viral protein.The approach of this study, providing high-resolution structural and kinetic information about a complex folding and binding interaction trajectory, can be applied to a number of experimental systems to provide a general framework for understanding conformational disorder in biomolecular function and could lead to the development of innovative anti-viral.
Press release (in french only)