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2019-10-29 - 5th FRISBI annual user meeting

the 4th of February at Gif sur Yvette, France

2019-10-29 - 5th FRISBI annual user meeting

4th of February 2020 at Gif sur Yvette, France

2019-06-05 - 1st French congress on Integrative Structural Biology (BSI-2019)

Jointly organized by AFC and SFB

2019-06-05 - 1st French congress on Integrative Structural Biology (BSI-2019)

Jointly organized by AFC and SFB

2019-03-20 - Potassium at the heart of protein synthesis

Essential for the vital functions of our body, protein synthesis takes place in our cells at the heart of ribosomes. Researchers from Gulnara Yusupova's team at the IGBMC (CNRS/Inserm/Unistra), in collaboration with Diamond Light Source in the United Kingdom, have identified potassium ions within the functional centres of bacterial ribosomes, a location previously attributed to magnesium ions. Published in Nature communication on March xx, these unexpected results provide a better understanding of the complexity of the structure and function of these large macromolecular complexes.


Genuine molecular machines, ribosomes decipher the information contained in a copy of DNA, called messenger RNA, to synthesize proteins. They "read" the messenger RNA triplets (mRNAs) from the transcription and select the appropriate transfer RNAs (tRNAs). These tRNAs carry amino acids which, when put together, constitute a protein. Ribosomes are thus able to "choose" the right tRNAs that correspond to mRNAs. Composed of proteins and ribosomal RNAs (rRNAs), these large complexes require metal ions to maintain their configuration in space but also to carry out protein synthesis. A role hitherto wrongly attributed to magnesium. Indeed, in the determination of high-resolution structure, the identity of a positive ion specifically linked to an RNA can be very ambiguous: is this drop of density a water molecule? A magnesium? Or anything else? Often a magnesium is placed by default. In recent years, it has become evident that many structures contain poorly assigned ions. This is the case for ribosomal structures.


In this study, thanks to long-wavelength X-ray diffraction, in collaboration with Diamond Light Source, and crystallography, Gulnara Yusupova's team, and in particular Alexis Rosov, also employed at Ribostruct*, were able to describe with unprecedented precision the complexity of the bacterial ribosome structure. They identified hundreds of potassium ions involved in the formation of the three-dimensional structure of rRNA, interactions between rRNA proteins and ribosomal protein structures. They also observed the presence of potassium ions in the functional centres of the ribosome, thus demonstrating their involvement in protein synthesis.


This data expands the fundamental knowledge of ribosome function and structure. This will benefit a large community of scientists interested in various aspects of protein synthesis, from the fundamental principles of ribosome action to pharmaceutical chemistry applications.


This study was funded by the ANR, the Foundation for Medical Research, the Russian government and the Federal University of Kazan.


* The teams of Gulnara Yusupova and Marat Yusupov have constantly improved their techniques and have acquired an undeniable know-how for the crystallization of the eukaryotic ribosome and the study of its functioning. Today, the resolution with which they are able to observe this structure is sufficiently precise for the development of new drugs targeting the eukaryotic ribosome. In 2015, they set up a start-up project, Ribostruct, led by Jean-Paul Renaud, to promote this know-how.

2019-02-13 - PSB Young Investigator Award

The Partnership for Structural Biology (PSB) of the EPN campus, Grenoble, France, is pleased to announce the creation of the PSB Young Investigator Award, which will be awarded biennially to give recognition to scientists having made exceptional contributions to research in structural biology that benefited from the PSB and its facilities. The PSB now invites nominations for the first edition to be awarded in July 2019 (deadline March 8th 2019).

The Award winner will receive a prize of 2000€ and will be invited to give a talk on their research at the PSB symposium which will take place on 4-5 July 2019 (travel and expenses paid).

For further information on the application process and eligibility criteria please check:

2019-02-13 - PSB Symposium “Macromolecules in action”

After the success of its first symposium on cryo-EM in 2017, the Partnership for Structural Biology (PSB) is pleased to announce a second symposium on "Macromolecules in action " which will take place on 4-5 July 2019 on the EPN campus, Grenoble, France.

Since its inception, structural biology has sought more detail at ever-improved resolutions. Methodological developments have since allowed structural analyses of macromolecular assemblies of increasing size and complexity. However, in order to fully understand the mechanistics and dynamics of complex cellular machineries, it is of crucial importance to place these interdisciplinary results  in an appropriate biological context using information from all resolution levels - from atomic detail to cellular and higher levels of organisation.

The aim of this meeting is to illustrate how the big biological questions are resolved by combining key methods in structural biology  (eg X-ray and neutron crystallography, cryo-EM, NMR and small angle scattering - SAXS and SANS) with other complementary approaches, enhancing our understanding of the dynamic behaviour of macromolecular complexes in the cell.

For further information and registration, please check here:

2019-02-05 - International PhD call 2019

We are most pleased to announce the Integrative Molecular and Cellular Biology (IMCBio) graduate school International PhD call 2019!


The IMCBio graduate school from the University of Strasbourg builds on the strong research developed in three Laboratories of Excellence (LabEx) INRT (Integrative biology: Nuclear dynamics, Regenerative and Translational medicine), MitoCross (Mitochondria-nucleus Cross-talk) and NetRNA (Networks of regulatory RNAs), which covers all areas of molecular and cellular biology at the levels of molecular factors, genes, cells and organisms from model systems to diseases. The combination of the three LabEx provides a unique opportunity to get a broad overview of every aspects of gene regulation covering nuclear organization, epigenetics, transcriptional, translational, post-transcriptional and post-translational events as well as crosstalks between the nucleus, cytoplasm and organelles in eukaryotes and cell-to-cell communication.


The complementarities and synergies between the LabEx researchers constitute an attractive training community for the future IMCBio PhD students. Trainees also benefit from outstanding technology infrastructures and platforms to develop high-level research projects in a stimulating and interdisciplinary environment.


If you are a highly motivated candidate of academic excellence and if you want to start an innovative research project in 2019, then click down below to candidate and join the IMCBio graduate school!

The application deadline for the 2019 call is March 22nd 2019 (noon time Paris)

2019-01-24 - Instruct Biennial Structural Biology Conference

Registrations are now open for the Instruct Biennial Structural Biology Conference to take place in Alcalá de Henares (near Madrid) 22-24 of May 2019. Confirmed speakers includes: Sjors Scheres, Julia Mahamid, Eva Pereiro, Andrej Sali, Teresa Carlomagno, Alex de Marco, Dave Stuart and H M Al-Hashimi. There are 10 fellowships available for graduate students which will cover travel and accommodation costs.  4 speakers will be selected from abstracts. Register now


There will be also a talk by the third Bertini award winner. The award recognises a significant achievement in frontier research that utilises an integrative structural biology approach. The award is the first commemorating Ivano Bertini who develop powerful new methods in NMR and built up the world class Centre for Magnetic Resonance in Florence. The award of €15000 is endowed by Bruker BioSpin and you can submit a nomination here

2018-12-04 - The largest yeast protein decoded at the atomic level

Ribosomes play an essential role in living things: they are the central sources of protein production in all types of cells. In eukaryotes, the assembly and maturation of these gigantic protein factories are initiated in the cell nucleus by various factors, including Rea1, which is the largest and most complex yeast protein. Thanks to cryoelectron microscopy, Helgo Schmidt's team at the IGBMC (CNRS/Inserm/University of Strasbourg) unveils the fine structure of the maturation factor Rea1. Published on 21 November 2018 in the journal eLife, this work makes it possible to visualize at the atomic scale one of the major mechanisms of ribosome maturation.

Real molecular machines, ribosomes decipher the information contained in a copy of DNA, called messenger RNA, to synthesize proteins. But how are ribosomes themselves produced? Their assembly is initiated in the nucleus where the proteins and RNAs constituting the large ribosomal subunit interact with more than 200 assembly factors. Ultimately, the large mature subunit is found in the cellular cytoplasm where it joins the small ribosomal subunit to form functional ribosomes. In order to promote the export of the large subunit from the nucleus to the cytoplasm, the Rea1 protein eliminates some of the assembly factors.


Rea1 is a huge protein of 5000 amino acids, which consists of a ring and a tail. At the ring level, the hydrolysis of ATP occurs, which allows the release of energy. This mechanism triggers a remodeling process in the tail, which in turn generates a mechanical force to eliminate assembly factors. Despite the crucial importance of ribosome maturation, the fine structure and mechanism of Rea1 remained largely enigmatic.


Using cryoelectron microscopy, the researchers were able to construct a detailed atomic model of Rea1, which revealed that an "arm" associated with the center of the ring regulates the hydrolysis of ATP. The "arm" also controls the formation of a binding site that allows Rea1 to interact with the assembly factors it must eliminate. In addition, the model revealed large portions of the tail of Rea1 and provided insights into a key question, namely how hydrolysis of ATP in the ring could cause tail remodeling.


All these results provide important information on the molecular architecture of the largest ribosome maturation factor.


This study was funded by a LabEx Chair (LabEx INRT),an ATIP-Avenir grant as well as a Région Grand Est jeunes chercheurs fellowship.

2018-11-23 - Launch of the IMCBio Graduate School

The IMCBio (Integrative Molecular and Cellular Biology) Graduate School aims to train a new generation of researchers interested in interfaces in biological sciences. The official launch of this innovative training project will take place in the presence of Michel Deneken, the President of the University of Strasbourg, Jules Hoffmann, winner of the 2011 Nobel Prize in Physiology and Medicine, together with members of the management of the State Major Investment Programmes at the National Research Agency, on Wednesday 28 November at 10am at the University Palace in Strasbourg. During this meeting, the various stages of the implementation of this major project and its objectives of training excellence through research will be presented.


Learning research by doing

Through multiple internships in laboratories, complementary training modules at master's level, summer schools, and a high-level doctoral training program, IMCBio aims to train students with a strong motivation for research to become future researchers interested in interfaces in biological sciences. With the joint support of the University of Strasbourg (Faculty of Life Sciences and Doctoral School of Life and Health), the CNRS and the Inserm, this project, which is based on the graduate school model, has three objectives: to strongly link training to research, to enhance the strengths of the scientific themes of Strasbourg and Illkirch sites and to contribute to its international influence.


An attractive training program

In this context, 17 students in their first year of Master's degree were selected for their first term in September 2018. "A successful and remarkable start to the school year,  says Bertrand Séraphin, Director of the Institute of Genetics, Molecular and Cellular Biology (IGBMC) and Project Director. We have received requests not only from French and foreign students who would like to join the course next academic year, but also from other institutions interested in this innovative teaching model.” Thanks to the support of the Faculty of Life Sciences of the University of Strasbourg, the first class of IMCBio students has already benefited from high-level scientific seminars in different disciplines. Nicolas Matt, co-director of the project and professor-researcher at the Institute of Molecular and Cellular Biology (IBMC, M3I), has planned to open the ethics seminar he organizes to all students in biology courses. "The budget of the graduate school allows us to invite researchers at the forefront of their field and we obviously want to make it available to the entire community," he asserts before adding: "There will also be training courses that will restricted to smaller numbers of students and will be reserved for IMCBio students.”

From 2019, the prestigious IMCBio programme will be open to doctoral students and should enable development of competitive research projects over three years. 



The IMCBio Graduate School

Based on a strategic grouping of Strasbourg's molecular and cellular biology strengths from three laboratories of excellence (LabEx INRT, NetRNA and MitoCross) with the help of state-of-the-art technological tools, five National Infrastructures in Health Biology (CELPHEDIA/PHENOMIN, FRISBI, France Genomics, Ingestem and IFB at the IGBMC) as well as the new insectarium (Equipex I2MC at the IBMC), this innovative training project with a budget of €6,282,000 is one of the four graduate schools winners supported by the University of Strasbourg.



Project Director: Bertrand Séraphin, Research Director, CNRS

Co-director of the project: Nicolas Matt, Senior Lecturer, University of Strasbourg

Project Coordinator: Pauline Vorburger,

LabEx representatives: INRT (Bertrand Séraphin), MitoCross (Ivan Tarassov), NetRNA (Pascale Romby)

2018-11-08 - Instruct Biennial Structural Biology Conference

Registrations are now open for the Instruct Biennial Structural Biology Conference to take place in Alcalá de Henares (near Madrid) 22-24 of May 2019. Confirmed speakers includes: Sjors Scheres, Julia Mahamid, Eva Pereiro, Andrej Sali, Teresa Carlomagno, Alex de Marco, Dave Stuart and H M Al-Hashimi. There are 10 fellowships available for graduate students which will cover travel and accommodation costs.  4 speakers will be selected from abstracts. Register now


There will be also a talk by the third Bertini award winner. The award recognises a significant achievement in frontier research that utilises an integrative structural biology approach. The award is the first commemorating Ivano Bertini who develop powerful new methods in NMR and built up the world class Centre for Magnetic Resonance in Florence. The award of €15000 is endowed by Bruker BioSpin and you can submit a nomination here

2018-10-24 - Instruct interships

6th Open Call for Instruct-ERIC Internships now open!


The Instruct Internship Programme funds research visits of 3-6 months duration to Instruct Centres in Europe. The aim is to facilitate valuable collaborations with Instruct research groups applying techniques that are not available in the applicant’s laboratory. Applications should specifically focus on the benefit to the applicant’s research. Internships may be hosted at any institution that hosts an Instruct Centre, providing the applicant is a resident of a different full Instruct member country at the time of making the application.

More info at

2018-02-13 - Observing protein activity in the nucleus of living human cells

Visualize without disturbing structures and processes taking place in the living cell nucleus is now possible thanks to an innovative technique developed by Laszlo Tora’s team at the IGBMC (CNRS/Inserm/Unistra) in close collaboration with Etienne Weiss at the ESBS Research Institute (CNRS/Unistra). This method allows to introduce, efficiently and without damaging the cells, antibodies labelled with small fluorescent molecules. In the cytoplasm of cells, these fluorescent antibodies bind to their antigens or targets. When the target is a nuclear protein, antibodies are transported with them into the nucleus, allowing researchers to locate and track the movements of this nuclear protein with high accuracy and in real time. The results of this study were published on February 12th, 2018 in the Journal of Cell Biology


Protein detection by immunofluorescence is a technique that has been widely used for many years, where proteins or their post translational modifications are identified with antibodies coupled to microscopically detectable fluorescent compounds. The disadvantage of this process is that the cells need to be fixed and permeabilized, which may damage them, to allow the entry of labelled antibodies. Furthermore, the need to fix cells does not allow the observation of the progression of a biological mechanism over time.


In this new study, researchers from Laszlo Tora’s and Etienne Weiss's teams have developed an ingenious method that allows them to observe chromatin-based mechanisms in the nucleus of living cells, without altering the observed processes. This technique allows the introduction of any antibody labelled with fluorescent compounds that bind specifically to nuclear factors into the cells by using an electric micro-shock that does not modify cells physiology. When these antibodies are in the cytoplasm, they bind to the nuclear factors produced in this cell compartment. Since these factors are naturally transported to the nucleus to exert their function, the nuclear factors linked antibodies are taken to the nucleus. "The antibodies, which bind to these newly synthesized factors, are transported in the nucleus of the cell like small backpacks and, as they are marked with fluorochromes of any color, they will send a signal which allows us to observe the nuclear factors to which they are linked", explains Laszlo Tora. In addition, this visualization of nuclear factors in living cells is very effective because each antibody can be labelled with five to seven fluorescent molecules. The treated cells were observed with a confocal microscope and, in collaboration with the Basel Imaging Centre, with a very high-resolution microscope, the 3D-SIM. Precise observation of proteins that have nuclear activity during the cell cycle allows to see their dynamics and motion in the nucleus of living cells. Researchers have also shown that this strategy makes it possible to detect in real time the appearance and management of DNA damages in the nucleus by detecting a post translational modifications. By using an antibody fragment that has the same properties as a complete antibody and targets a major actor in triggering DNA repair (gammaH2AX), researchers were able to reveal areas in the nucleus where cell DNA is damaged by a substance causing genome changes, called genotoxic agent.


Given the large number of antibodies available on the market, this simple and innovative method will undoubtedly provide new information about nuclear proteins and a better understanding of their behavior in transmitting and maintaining the integrity of genetic information.


This study was funded by the ANR, ERC and the Regional League Against Cancer.

2017-11-15 - Visualization of chemical modifications in the human 80S ribosome structure

Chemical modifications of human ribosomal RNA (rRNA) are introduced during biogenesis and have been implicated in the dysregulation of protein synthesis, as is found in cancer and other diseases. However, their role in this phenomenon is unknown. Here we visualize more than 130 individual rRNA modifications in the three-dimensional structure of the human ribosome, explaining their structural and functional roles. In addition to a small number of universally conserved sites, we identify many eukaryote- or human-specific modifications and unique sites that form an extended shell in comparison to bacterial ribosomes, and which stabilize the RNA. Several of the modifications are associated with the binding sites of three ribosome-targeting antibiotics, or are associated with degenerate states in cancer, such as keto alkylations on nucleotide bases reminiscent of specialized ribosomes. This high-resolution structure of the human 80S ribosome paves the way towards understanding the role of epigenetic rRNA modifications in human diseases and suggests new possibilities for designing selective inhibitors and therapeutic drugs.

This work was carried out using a high resolution electronic cryo-microscope (Titan Krios) within the French and European infrastructures, FRISBI and Instruc-ERIC

2017-11-15 - Visualization of modifications in the human ribosome structure, a new feat for cryo electron microscopy

Ribosomes play a vital role in living beings: they are protein production stations in all cell types. These large complexes are made up of two kinds of molecules: proteins and ribosomal RNA (rRNA). Through structural studies, Bruno Klaholz's team at the IGBMC revealed more than 130 chemical modifications of the rRNAs. Published in the journal Nature on November 15 2017, these results not only provide a better understanding of the structural and functional roles of human ribosome modifications, but also open up new therapeutic pathways for the treatment of pathologies such as cancer or certain genetic diseases in which dysregulation of protein synthesis is involved.

Genuine molecular machines, ribosomes decipher the information contained in a copy of DNA, called messenger RNA, to synthesize proteins. During ribosomes biogenesis, chemical modifications occur at precise locations of rRNAs. The alteration of these modifications is sometimes associated with disruptions in protein synthesis. Moreover, these modifications in the rRNA structure seem to modulate the activity of antibiotics, indicating that they can influence the ribosome interaction with this kind of drugs.


Chemical modifications of rRNA have been known for decades, particularly in microbes, but their observation remained difficult. In this study, Bruno Klaholz's team at the IGBMC determined the localization and three-dimensional structure of 136 various types of modifications (methylations, acetylations, etc.) of human ribosome rRNAs. The researchers have thus uncovered the role of these chemical modifications which consists in stabilizing the rRNA structure.

The researchers also analyzed the structure of three antibiotics-binding sites, revealing that these molecules are either in direct contact or very close to the rRNAs modifications sites, implying a role of these modifications in the mechanism of action and specificity of these inhibitors. Moreover, the unexpected presence of certain rRNA modifications suggests that rRNA modifications in human ribosomes could vary between different cell types, especially between normal cells and cancer cells, and could thus constitute a signature for cancer states.

This study represents a major result made possible by cryo electron microscopy, a revolutionary method for the observation of macromolecules coupled with image processing and 3D reconstruction, by which the researchers were able to construct a detailed atomic model of the human ribosome. Recognized recently by the Nobel Prize in Chemistry 2017, this technique provides the double advantage of being able to study biological samples without altering their properties and also allows to fix the orientation of the objects to enable a 3D reconstruction. This work was carried out using a high-resolution electron microscope (Titan Krios) within the French and European infrastructures, FRISBI and Instruct, hosted at the Centre for Integrative Biology at IGBMC.


Beyond mapping at the atomic level, the visualization of rRNA chemical modifications provides unprecedented insights into their role in the stabilization of rRNA structure, in the translation process and in diseases related to ribosome dysfunctions, paving the way for the development of new drug.

This study was supported by the INCa, the Ligue, the ANR, the CPER 2007-2013 (the Greater Region, the Eurometropole of Strasbourg, the General Council of the Bas-Rhin, the Ministry of National Education, higher education and research), FRM, Inserm, CNRS, FRISBI and Instruct-ERIC.


2017-10-09 - Electron cryo-microscopy is honored!

The Sweden Nobel Prize in Chemistry 2017 was awarded to Switzerland's Jacques Dubochet, the German-born American Joachim Frank and Britain's Richard Henderson for developing electronic cryo-microscopy, a revolutionary molecular observation method coupled with 3D reconstruction. This technique allows not only to study biological samples without altering their properties, as it is the case with dyes, but also to produce high-resolution three-dimensional structures of biomolecules which represents a revolution in the field of structural biology.


FRISBI open access to national and international scientific, academic and industrial scientific communities to cryo-microscopy devices of high technology: Polara and Titan Krios, see our platforms catalogue

2017-07-19 - Instruct-ERIC was launched at a ceremony in London

At a Royal Society awards ceremony celebrating the prestigious new European Commission-approved status for structural biology Instruct Research Infrastructure, UK Minister for Universities, Science, Research and Innovation Jo Johnson recognised the value and relevance of collaborative work between the UK and European scientists.

2017-07-18 - Innate immunity: a new signaling pathway

The defense of an organism depends on its ability to recognize danger signals. In mammals including humans, macrophages represent a predominant cellular system that acts against pathogens and removes cellular debris. Activation of macrophages represents a crucial immune defense mechanism and its deregulation contributes to uncontrolled inflammation and autoimmune diseases. Romeo Ricci’s team at the IGBMC has identified a new signaling pathway involved in the intracellular innate immune defense system. For the first time, they provided evidence that the Golgi apparatus, an important cellular organelle, is involved in the activation of the inflammasome, an intracellular multiprotein complex capable of sensing tissue damage and infectious agents. They also showed that pharmacologic interference with this newly identified mechanism can be used to mitigate inflammation. This study was published on 17 July 2017 in the Journal of Experimental Medecine (JEM).


The macrophage harbors two defense systems against dangers signals: on the one hand, specific receptors on their membrane surface and, on the other hand, intracellular complexes including the the various subsets of inflammasomes that are subjects of this study.


Romeo Ricci’s teamwas particularly interested in the NLRP3 inflammasome subunit activation mechanism. NLRP3 has been recently shown to directly bind to mitochondria-associated endoplasmic reticulum membranes (MAMs) allowing for inflammasome activation. This work showed for the first time that the Golgi apparatus activates Protein Kinase D (PKD) leading to NLRP3 phosphorylation. This phosphorylation was essential to release NLRP3 from MAMs resulting in recruitment of additional components and assembly of the mature NLRP3 inflammasome in the cytoplasm triggering an inflammatory response.

Patients affected by a rare genetic disease called CAPS, in which the gene encoding for the NLRP3 protein is mutated, the NLRP3 inflammasome is constitutively activated resulting in auto-inflammation. Using immune cells isolated from these patients, they demonstrated that inhibition of PKD blocked NLP3 inflammasome activation in vitro and mitigated release of pro-inflammatory factors providing a solid basis for new treatment options in NLRP3-related inflammatory diseases.



The study was funded by a USIAS fellow grant from the University of Strasbourg and the European Research Council (ERC).

2017-07-05 - Instruct-ERIC decision adopted

The European Commission adopted the Instruct-ERIC decision on the 4th July 2017. Instruct is the 17th ERIC to be adopted.

Instruct was initiated in 2008 as a European-funded Preparatory Phase Project 211252 in the ESFRI Programme. In 2011, Instruct entered a transitional phase and in 2012 was operational, providing the first access to Instruct infrastructure through its Centres. Instruct has grown to provide new infrastructure, now modes of service delivery, excellent training courses and internships and has supported scientists through its R&D Pilot programme. Instruct-ERIC will provide the stability and sustainability for Instruct services to the structural biology community and to other life sciences communities within Europe.

Instruct was awarded an EU-funded project 'Instruct-ULTRA' in 2017 to further expand Instruct membership and services. Instruct-ULTRA will enable Instruct to work with new communities and extend and evolve the Instruct infrastructure to meet the demand of researchers wanting high quality structural technologies and methods.

In the nine years of Instruct development, there have been many people who have contributed and this success is thanks to them. Congratulations to all who played their part and we look forward to a bright and productive future as Instruct-ERIC.

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