2010

2010 ERC Starting Grant for Jerome Boisbouvier

Jerome Boisbouvier, researcher in the Biomolecular NMR spectroscopy Group at the IBS has been awarded a Starting Grant by the European Research Council (ERC).
His project, SeeNanoLifeInAction, aims to study real-time biological nanomachines in action by NMR.
More details on his career and his project are available here (in french only).

Biosynthesis of the bacterial cell wall

The bacterial cell wall is a three-dimensional structure that protects the cell against environmental stresses and also ensures its shape. The synthesis of peptidoglycan, the major component of the cell wall, requires the cooperation of several proteins, and the sheer complexity
of the process constitutes a major problem for the study of its regulation and assembly of its components. Researchers from the Bacterial Pathogenesis Group have collected new structural and biochemical data on several components of the assembly machinery of the peptidoglycan issued from different pathogens, and provide new insights into this molecular machinery.

Bridging cell wall biosynthesis and bacterial morphogenesis. Matteï P-J, Neves D and Dessen A. Current Opinion in Structural Biology 20(6) : 749-755 ou 766

Some enzymes are the prisoners of a molecular cage !

The structure of a Regulatory ATPase Variant protein (MoxR AAA+) found in E. Coli reveals the design principles of a molecular cage modulating the inducible lysine decarboxylase activity. This enzyme stabilizes the pH inside the cell by liberating the carboxyle group of the lysine thus allows the bacteria to resist to different stress.
This work has been initiated in the Department of Biochemistry of the University of Toronto, in collaboration with the UVHCI. The program VEDA has been used for fitting molecular model into electron microscopy reconstruction allowing the interpretation of the data (contact G.Goret, IBS).

Structure of RavA MoxR AAA+ protein reveals the design principles of a molecular cage modulating the inducible lysine decarboxylase activity.
El Bakkouri M, Gutsche I, Kanjee U, Zhao B, Yu M, Goret G, Schoehn G, Burmeister WP, Houry WA.
Proc Natl Acad Sci U S A. ;107(52):22499-504.

Structural biology : Proteins in dynamic equilibrium

Protein molecules in solution exist as an equilibrium of different conformations. These different conformations and their proportions can not be studied by classical methods of structural biology. A report by the researchers from the Protein Dynamics and Flexibility by NMR Group shows how they can be measured in solution by NMR and small angle scattering. This article underlines the need to take into account the dynamics to better understand molecular biology.

Structural biology : Proteins in dynamic equilibrium. Bernadó P, Blackledge M. Nature ;468(7327):1046-8.

Relocation of Aurora B and survivin from centromeres to the central spindle impaired by a kinesin-specific MKLP-2 inhibitor

The chromosome passenger protein complex (CPC composed of Aurora B kinase, survivin, INCENP and borealin) is localized in the inner centromeres of sister chromatides during mitosis. The proteins of CPC are implicated in the spindle assembly checkpoint correcting the faulty attachments of spindle microtubules (MT) with the kinetochores. In anaphase, the loss of sister chromatide cohesion provokes the departure of the CPC from the centromeres to the spindle midzone MTs where the play an important role in cytodieresis. The migration of the CPC into the central spindle is dependent on the activity of a MT-based motor protein MKLP-2. Our paper describes the identification and characterization of the first specific inhibitor of MKLP-2. A library of 8 900 small molecules was screened for inhibition of the ATPase activity of MKLP-2 resulting to the identification of a small molecule inhibitor of MKLP-2, which we named paprotrain (PAssenger PROteins TRAnsport INhibitor). The inhibitor was uncompetitive with ATP and did not bind to the MT binding site of the MKLP-2 motor domain. Most importantly, the inhibitor was also able to target specifically MKLP-2 in cells by inhibiting the migration of CPC to the central spindle causing cytokinetic defects. The inhibitor will be a useful tool for chemical genetics to study the function of MKLP-2 in cytokinesis and to gain mechanistic insights, for example to exploit mechanistic differences between the various kinesins.

Relocation of Aurora B and survivin from centromeres to the central spindle impaired by a kinesin-specific MKLP-2 inhibitor. Tcherniuk S, Skoufias DA, Labriere C, Rath O, Gueritte F, Guillou C, Kozielski F. Angew Chem Int Ed Engl. 2010 Oct 25 ;49(44):8228-31.

Consequence of MKLP-2 inactivation

MKLP-2 inactivation by a specific small molecule inhibitor leads to a failure in the recruitment of a chromosome passenger protein (survivin in red) to the central spindle (microtubules in green) during anaphase chromosome segregation (DNA in blue).

More than the sum of its parts

Novel hybrid compounds consisting of an organic β-sheet-breaking moiety and a signaling, D-enantiomeric Aβ-recognizing peptide moiety have been designed (see picture). The compounds, which were chemically synthesized and characterized by several techniques, combine rational design and drug selection from libraries and inhibit Aβ oligomerization and Aβ-induced synaptic pathology.

Combining independent drug classes into superior, synergistically acting hybrid molecules.
Müller-Schiffmann A, März-Berberich J, Andreyeva A, Rönicke R, Bartnik D, Brener O, Kutzsche J, Horn AH, Hellmert M, Polkowska J, Gottmann K, Reymann KG, Funke SA, Nagel-Steger L, Moriscot C, Schoehn G, Sticht H, Willbold D, Schrader T, Korth C.
Angew Chem Int Ed Engl. ;49(46):8743-6.

Unraveling K-turn RNA structure by a combination of NMR and small angle scattering

In a collaboration with Dr. Teresa Carlomagno’s NMR laboratory at EMBL Heidelberg, Frank Gabel (LBM/IBS) has contributed to the first structural investigation at atomic resolution of an unbound K-turn RNA (the spliceosomal U4-Kt RNA) by a combination of NMR and small-angle neutron scattering (SANS). The concerted use of both techniques presents a very powerful methodological approach to complement the short-range (atomic or residue) structural information from NMR with long-range distance restraints from SANS.
K-turn motifs are universal RNA structural elements providing a binding platform for proteins in several cellular contexts and represent an example of a three-dimensional architectural RNA motif. Such motifs are increasingly recognized as determinants of RNA functionality. The free RNA K-turn structure presented here together with previously published protein bound structures contributes to build the basis for understanding sequence–structure and structure–function relationships in RNA, and to characterize the conformational landscape of this exquisitely flexible and adaptive molecule.

Structure of the K-turn U4 RNA : a combined NMR and SANS study. Falb, M., Amata, I., Gabel, F., Simon, B. and Carlomagno, T. Nucleic Acids Res. 38(18), 6274-6285.

A new target for cancer drugs

A new mode of action of ellipticine, a molecule known for its anti-cancer properties has been identified by scientists from the CEA, CNRS, INSERM, Institut Curie and Joseph Fourier-Grenoble1 University. They selected derivatives of this molecule capable of specifically targeting the CK2 protein, a protein kinase2 deregulated in many cancers and demonstrated the antitumor potential of these derivatives. This work, published online by Cancer Research, opens new perspectives for the design of future cancer drugs.

Press release

(in french only)

Antitumor activity of pyridocarbazole and benzopyridoindole derivatives that inhibit protein kinase CK2.
Renaud Prudent, Virginie Moucadel, Chi-Hung Nguyen, Caroline Barette, Frédéric Schmidt, Jean-Claude Florent, Laurence Lafanechère, Céline F. Sautel, Eve Duchemin-Pelletier, Elodie Spreux, Odile Filhol, Jean-Baptiste Reiser, and Claude Cochet.
Cancer Research, 70(23):9865-74.

Science Fair 2010

  From October 21 to 22, 2010, the IBS invited high school students to discover the world of proteins and the techniques used to probe the infinitely small :
To probe the mysteries of life at the atomic scale, special methods and facilities are needed. IBS scientists explained these and help a hundred school pupils perform scientific experiments in their labs.

 From October 21 to 22, 2010, IBS scientists invite primary school pupils to explore the world of the living at the atomic scale :
In a two hour session, scientists and technicians demonstrated the methods used to investigate the mysteries of life. A hundred pupils were first invited to participate in one of three workshops (short experiments involving proteins and DNA) followed by group visits to the laboratory to discover the different instruments used to study the world of the infinitely small.

- From October 21 to 24, 2010, IBS scientists also welcomed a large family audience at the science Village in Grenoble
Our staff animated a game to explain its activities and illustrate the diversity of life.

About fifty volunteers (almost 20% of IBS staff) were mobilized to welcome secondary school pupils and the lay public and helped to make it a successful event.

A prize from the French Academy of Sciences awarded to Carlo Petosa (MMIP group leader)

Each year, the French Academy of Sciences distributes about 80 prizes. The 2010 Montyon price was awarded to Carlo Petosa, MMIP group leader at the IBS.

Artificial Metalloenzymes or tomorrow synthetic chemistry

Scientists from the CEA, the Université Joseph Fourier and the CNRS have recently developed a now approach combining protein crystallography and biomimetic chemistry to observe all the steps in oxygen activation, an essential reaction of life. In order to accomplish this, they have designed and crystallized an artificial metallo-enzyme consisting of a synthetic catalyst and a protein. The different states have been characterized by X-ray diffraction at the European Synchrotron Radiation Facility (ESRF). These results are an important step towards the design of artificial metallo-enzymes capable of synthetizing many industrially relevant molecules, both efficiently and at lower costs. This work, that opens new alternatives for a "green" chemistry approach has been published in the journal Nature Chemistry.

Crystallographic snapshots of the reaction of aromatic C–H with O2 catalysed by a proteinbound iron complex. Christine Cavazza, Constance Bochot, Pierre Rousselot-Pailley, Philippe Carpentier,
Mickaël V. Cherrier, Lydie Martin, Caroline Marchi-Delapierre, Juan C. Fontecilla-Camps and Stéphane Ménage. Nature Chemistry, 2 : 1069–1076

Bacterial cell wall observed by solid state NMR

Researchers from the IBS, in collaboration with INAC, Newcastle University and the University of Liege, have characterized and compared the organization and dynamics of the cell wall of different bacterial species by solid state NMR. Rapid identification by NMR of molecular structures, in particular teichoïc acids, found on the surface of various strains and mutants, will help to identify genes and mechanisms involved in virulence. This work paves the way for studying the surface of other cell types and the observation of cell contacts during host/pathogen interactions.

Dynamics characterization of fully hydrated bacterial cell walls by solid-state NMR : evidence for cooperative binding of metal ions.
Kern T, Giffard M, Hediger S, Amoroso A, Giustini C, Bui NK, Joris B, Bougault C, Vollmer W, Simorre JP.
J Am Chem Soc. 11 ;132(31):10911-9.

Light can repair what light has damaged

UV-damage to DNA is potentially lethal to cells but can be handled by a dedicated enzyme, DNA photolyase which, most ingeniously, uses visible light for direct reversion of the most current lesions. The review discusses the reaction mechanisms of this flavoprotein.

Reaction mechanisms of DNA photolyase. Brettel K and Byrdin M
Current Opinion in Structural Biology ; 20(6):693-701

New potent and dual inhibitors of kinases involved in cancer cell proliferation and survival

The casein kinase 2 (CK2) and Proviral Insertion Moloney virus kinases (Pim kinases) are serine/threonine kinases that have key roles in a wide variety cellular processes including cell differentiation, proliferation and survival. Very interestingly, they act on similar but not redundant pathways involved in tumorgenesis, making simultaneous inhibition relevant cancer therapy in particular for treatment of leukaemia, prostate cancer and lymphomas.
The collaboration between IBS (J.-B. Reiser, Grenoble), the Institut Curie (F. Schmidt, Paris), INSERM and iRTSV-CEA (C. Cochet, Grenoble) and Oxford university (S. Knapp, Oxford UK) has allowed to identify and to characterize new potent and dual inhibitors for CK2 and Pims that are unrelated to previous described compounds.
The difurane family is thus a new and very expected lead in optimization of cell-potent and dual inhibitors targeting pathological signal pathways that control apoptosis resistance and growth regulation of cancer cells.

New potent dual inhibitors of CK2 and Pim kinases : discovery and structural insights. Lopez-Ramos M, Prudent R, Moucadel V, Sautel CF, Barette C, Lafanechere L, Mouawad L, Grierson D, Schmidt F, Florent JC, Filippakopoulos P, Bullock AN, Knapp S, Reiser JB and Cochet C. Faseb Journal 2010 Sep ;24(9):3171-85

Fifth scientific day and a new logo for IBS

The fifth IBS scientific day was held on June 28 on the Saint Martin d’Heres Campus. Nearly 150 members were present to listen to four plenary lectures and communications by four students belonging to one of the four research themes of the institute (program). A presentation was made of our actions for the Science Fair since 2004, as well as the workshops planned for the 2010 edition (details).

In addition, participants could read twenty posters submitted by PhD students.

And last but not least, the IBS logo was presented :

NatX-ray creates NatX-ray LLC in the USA

Launched in April 2009, based on research carried on in Jean-Luc Ferrer’s team (IBS, Grenoble), NatX-ray SAS company just created NatX-ray LLC, a US subsidiary. This subsidiary is dedicated in a first time to the commercialization of consumables for crystallography. NatX-ray LLC is installed in San Diego, California, to take advantage of the proximity of famous research institutes involved in protein crystallography, such as the Salk Institute, the Scripps Institute, the Burnham Institute, La Jolla Institute for Allergy and Immunology as well as pharmaceutical companies (Novartis, Pfizer, ...) and biotech companies (Illumina, Active Sight, ...). This area offers already a significant market for NatX-ray products, and is the perfect starting point to reach the rest of the US market.

Atomic description of HIV-1 protease enzyme in-action

The three dimensional structure of a complex between active HIV-1 protease and a substrate oligopeptide, converted in-situ into a tetrahedral reaction intermediate(TI), has been determined using data to 1.76 Å resolution collected on the FIP-BM30A beamline at the ESRF. In this snapshot of the enzyme in-action, the TI and one of the two catalytic aspartates are engaged in a very short hydrogen bond, which gives an insight into enzyme mechanism.

X-ray snapshot of HIV-1 protease in action : observation of tetrahedral intermediate and short ionic hydrogen bond SIHB with catalytic aspartate. Das A, Mahale S, Prashar V, Bihani S, Ferrer JL and Hosur MV. Journal of the American Chemical Society (2010) 132(18) : 6366-6373

Regulation of protease activity : when C1 inhibitor cooperates with heparin

C1 inhibitor is a regulatory protein that controls the activity of several blood proteases involved in particular in innate immunity (complement system) and blood coagulation. Its reactive SERPIN (SERine Protease INhibitor) domain has been successfully produced in a recombinant form and characterized functionally using different methods, providing evidence that heparin potentiates its inhibitory activity towards proteases through an unusual « sandwich » mechanism. These data shed light on the mechanism of action of this inhibitor which plays a key role in the control of inflammation

Functional characterization of the recombinant human C1 inhibitor serpin domain : insights into heparin binding. Rossi V, Bally I, Ancelet S, Xu Y, Frémeaux-Bacchi V, Vivès RR, Sadir R, Thielens N, Arlaud GJ. J Immunol, 184 : 4982-4989.

Eva Pebay-Peyroula appointed Chairwoman of the National Research Agency (ANR)

Eva Pebay-Peyroula has been chosen to succeed Jacques Stern as President of the National Research Agency (ANR), the French national funding agency for research projects.
Professor at the University Joseph Fourier, director of the IBS since 2004, CNRS Silver Medal 2005, Mrs Pebay-Peyroula is a member of the Academy of sciences of the Institute of France. Her research focuses on the contribution of structural biology to understand the functions of membrane proteins.

A new Isotope Labelling Approach for Direct Detection of CH/π Interactions in Protein

Researchers from the NMR group at the Institut de Biologie Structurale have reported the first direct experimental evidence of biological XH/π interactions, a weak hydrogen bond-like interaction long believed to contribute to biomolecular structure and function. XH/π interactions are weaker than canonical hydrogen bonds and are commonly identified indirectly from high resolution 3D structures. Through the use a new, ultra-sensitive isotope labelling approach (also developed at the IBS) NMR researchers were able to detect these weak interactions using 2D heteronuclear NMR experiments. With this approach they were able to unambiguously identify the corresponding donor and acceptor groups and detect XH/π interactions not previously predicted from 3D structural models.

Direct detection of CH/pi interactions in proteins. Plevin MJ, Bryce DL, Boisbouvier J. Nat Chem. 2:466-71.

Stereospecific isotopic labeling of methyl groups for NMR spectroscopic studies of high-molecular-weight proteins. Gans P, Hamelin O, Sounier R, Ayala I, Dura MA, Amero CD, Noirclerc-Savoye M, Franzetti B, Plevin MJ and Boisbouvier J. Angewandte Chemie International Edition, 49 : 1958-1962

The low temperature inflection in neutron scattering measurements of proteins is due to methyl rotation

The dynamic nature of protein structures is essential for macromolecular function and biological activity. Like in a motor operating
at full speed, a multitude of motions on various length and time scales characterize a protein at work. At physiological temperatures, protein dynamics are rich and complex. At decreasing temperatures, protein motions slow down or vanish, and the various protein
motions can be dissected and studied separately.
In a collaborative effort, scientists from the IBS, the ILL, the MPI in Martinsried, Germany, the University of Groningen, The Netherlands and the University of California in Irvine,USA have studied the nature of proteinmotions in the membrane protein bacteriorhodopsin at very lowtemperatures. In order to tackle the complexity of protein motions, several complementary biophysical and biochemical methodologies had to be applied, including neutron scattering, molecular dynamics simulations, NMR and specific protein
deuteration.
Results suggest that methyl groups are a major source of protein flexibility in that temperature range. Molecular dynamics simulations quantitatively reproduced the neutron results and NMR data showed that it is the methyl group rotation that is observed by neutron scattering in proteins at cryo-temperatures. Providing deeper insight into the complex nature of protein dynamics will
benefit rational drug design [To know more].

The low temperature inflection in neutron scattering measurements of proteins is due to methyl rotation : direct evidence using isotope labelling and molecular dynamics simulations.
J Am Chem Soc. Wood, Tobias, Kessler, Gabel, Oesterhelt, Mulder, Zaccai & Weik ;132(14):4990-1

Fight against HIV : a promising compound

At the Institut de Biologie Structurale, researchers have developed a molecule capable of blocking the transfer of HIV from one cell to another. This molecule has been the subject of a patent and a publication in the journal ACS Chemical Biology. It works by saturating a receptor called DC-SIGN, used by HIV to be transported in the body [Press release]

Inhibition of DC-SIGN Mediated HIV infection by a linear trimannoside mimic in tetravalent presentation. Sattin S, Daghetti A, Thépaut M, Berzi A, Sanchez-Navarro M, Tabarani G, Rojo J, Fieschi F, Clerici M, Bernardi A. ACS Chem Biol. ;5(3):301-12.

Interview RFI (in french only)

A new labeling strategy to study complex biomolecules by NMR

NMR Spectroscopy of large protein assemblies necessitates targeted protonation of specific sites within a perdeuterated background. Researchers of IBS and IRTSV outline the use of an acetolactate precursor for the specific biosynthetic incorporation of 13C1H3 into the pro-S methyl groups of leucine and valine. This labeling strategy enhances spectral quality and provides an efficient basis for the application of solution-state NMR techniques to complex biomolecules.

Stereospecific Isotopic Labeling of Methyl Groups for NMR Spectroscopic Studies of High Molecular Weight Proteins.
Pierre Gans, Olivier Hamelin, Remi Sounier, M. Asunción Durá, Marjolaine Noirclerc-Savoye, Carlos D. Amero, Bruno Franzetti, Michael J.Plevin & Jérôme Boisbouvier.
Angewandte Chemie International Edition, 49 : 1958-1962

Hybrid Potential Simulations of Post-Transfer Editing in Aminoacyl-tRNA Synthetases

Aminoacyl-tRNA synthetases (aaRSs) are critical for the translational process, catalyzing the attachment of specific amino acids to their cognate tRNAs. To ensure formation of the correct aminoacyl-tRNA, and thereby enhance the reliability of translation, several aaRSs have an editing capability that hinders formation of mis-aminoacylated tRNAs. In a collaborative effort, groups at the Universities of Tokyo and Tsukuba in Japan and at the IBS have investigated theoretically the mechanism of the editing reaction using ab initio hybrid quantum chemical/molecular mechanical potentials in conjunction with molecular dynamics simulations. It was found that the mechanism of the editing reaction for a class I enzyme, leucyl-tRNA synthetase (LeuRS), complexed with a mis-aminoacylated tRNALeu, was a self-cleavage reaction of the tRNA. Analysis of existing experimental data and additional modeling suggests that ribozymal mechanisms of this type could also occur in the ribosome, as well as in other aaRSs. Although the protein does not participate directly in the chemical reaction, it was shown to have important stabilizing effects on some of the high-energy intermediates along the reaction path. Such hybrid catalysts are also indicative of the transitional forms that could have played an important role in the RNA world hypothesis for the origin of life.

The Editing Mechanism of Aminoacyl-tRNA Synthetases Operates by a Hybrid Ribozyme/Protein Catalysis. Y. Hagiwara, O. Nureki, M. J. Field and M. Tateno. Journal of the American Chemical Society, 132(8):2751-8..

A new building for the Institut de Biologie Structurale

From its initial size of 100 people, the IBS has grown to an institute of over 220 individuals. It currently accomodates a start-up company and has plans to recruit young new international research teams. This steady growth made it necessary to envisage an expansion of the building and was accompanied by a desire for closer proximity to the other PSB institutes*.

A first step was taken in 2006, when a request for funding was filed with the state/regional granting agency CPER. This was followed by a lengthy series of internal discussions, meetings with the three organizations that jointly operate the IBS (the CEA, the CNRS and the University Joseph Fourier), and negociations with the PSB partners and with local politicians. Thanks to strong support from the three operating organizations and from the director of the CEA-Grenoble, the end of 2009 saw two major hurdles overcome : land for a new building was acquired on the joint ESRF/ILL campus (recently renamed the “EPN campus”), and the funds needed to finance the project were secured.

The new building, which was selected through competition, will have five floors and contain 8 000 m² of usable laboratory and office space. It will combine aesthetic architecture, a practical design intended to facilitate everyday research, and outstanding energy performance. After a period of detailed study, the request for a building permit will be submitted in July 2010, and work will begin in March 2011. The institute is scheduled to move into its new premises in spring 2013.

Vue d’architecte / Architects view of the futur IBS building

* Other PSB members include the European Synchrotron Radiation Facility (ESRF - one of the world’s most powerful sources of X-rays), the Institut Laue Langevin (ILL - the world’s leading neutron source), the European Laboratory of Molecular Biology (EMBL)

Accessing the Unfolded part of the Proteome from NMR : A Step Forward in Structural Biology

The central dogma that has motivated massive worldwide investment in structural genomic projects has been founded upon the assumption that the resolution of the three dimensional structure of a finite number of proteins will provide the key to understanding biological activity.

However, over the last decade it has become increasingly clear that a large fraction (up to 40%) of the proteins encoded by the human genome are intrinsically disordered or contain disordered regions of significant length. These intrinsically disordered proteins (IDPs) are functional despite a lack of a stable structure. The classical structure-function paradigm therefore breaks down for this class of proteins, and new insight into the relationship between primary sequence and molecular function is required.

The importance of developing new methodology to study these proteins is underlined by the fact that IDPs are associated with many human diseases, including cancer, cardiovascular disease, amyloidosis, neurodegenerative disease and diabetes. Vital molecular processes, their function, malfunction and potential inhibition by pharmaceutical agents, have escaped our attention for decades, and will continue to do so, unless we can develop the tools to study these elusive proteins.

The development of meaningful descriptions of the conformational behavior of IDPs therefore represents a key challenge for contemporary structural biology. Recent advances at the Institut de Biologie Structurale (CEA-CNRS-UJF) in Grenoble using Nuclear Magnetic Resonance spectroscopy demonstrate that atomic resolution understanding of the behaviour of these proteins can be derived from the simplest NMR measurements, chemical shifts. Chemical shifts are uniquely dependent on local conformational sampling, and in this study it is shown that explicit consideration of the dynamic averaging of chemical shifts provides an accurate description of the ensemble of conformers present in solution.

This breakthrough raises a long-standing, and fundamental barrier to our understanding of these intriguing proteins, and offers the very real prospect of following the conformational behavior of IDPs under conditions approaching those found in vivo, such as in crowded or even cellular environments.

Defining Conformational Ensembles of Intrinsically Disordered and Partially Folded Proteins Directly from Chemical Shifts. M.R. Jensen, L. Salmon, G. Nodet and M. Blackledge. J Am Chem Soc, 132(4) : 1270-2

J. Boisbouvier and J. Joly received the CNRS Bronze medal and the CNRS Crystal

On Monday January 18, 2010, Jerome Boisbouvier (IBS/LRMN) received one of the CNRS’s 2008 Bronze Medals for its studying of macromolecular assemblies by NMR.
And Jacques Joly (IBS/LCCP) received one of the CNRS’s Crystals 2009, for its work on the FIP beamline at the ESRF.

CNRS Bronze medals are meant to reward an ongoing and fruitful research activity and represents an encouragement from the CNRS to pursue it. About 50 bronze medals are awarded annually.

CNRS Crystals are given annually to a dozen engineers, technicians and administrative staff of the CNRS for their creativity and innovative contribution to research.