cometadata/datacite-titles-descriptions-related-identifiers huggingface dataset:
DOI: 10.15151/esrf-es-735812189
title: FInnish National Protein Crystallography Consortium

description: The Finnish BAG encompasses 25 groups active in crystallography in Finland. The projects vary widely and include membrane proteins such as membrane pyrophosphatases, and various protein complexes and receptors (growth factor receptors, integrins), signaling proteins such as kinases, other proteins involved in disease and antibiotics development (neuronal adhesion and myelin proteins, PP2A, ADP-ribosylation and biocatalytic enzymes) and several pathogen proteins (e.g. viral proteins) and various enzyme targets and e.g. studies on phytochrome photoreceptors and complexes involved in actin and cytoskeleton dynamics and regulation. Overall the BAG serves the national needs for highly variable projects, with different biological and biotechnological applications. Several project will benefit from microfocus beam lines and tunable wavelength options for phasing, others benefit from quick robust screening by MASSIF. Biology lab is needed for SAXS experiments.
DOI: 10.15151/esrf-es-736506304
title: Macromolecular Crystallography in Bordeaux/Lyon/Toulouse IECB IBGC CBMN / IBCP-MMSB ICBMS / IPBS

description: The different research teams who are part of this BAG are located in Bordeaux, Lyon and Toulouse. They are mainly working on worldwide health concerns or biotechnological relevant projects. In more details, infectiology, molecular assemblies, biosynthetic pathways or glycobiology are their main research axises. Important results have been obtained so far regarding the development of new therapeutic strategies against several infectious diseases or regarding plastic bioremediation. In order to go further into details of all these studies, access to ESRF facilities is a requirement.
DOI: 10.15151/esrf-es-643877202
title: Structural Biology BAG - Portugal

description: The Portuguese MX BAG includes 13 PIs from three different institutions. Our research interests include soluble and membrane proteins of biomedical interest from humans or pathogenic organisms, many of which can be drug targets. Focus is also given to structural enzymology, aimed at the elucidation of reaction mechanisms, active sites, and inhibition tolerance in proteins with potential biotechnology applications. In several cases, complementary structural biology approaches are being used, combining MX with SAXS and, more recently, CryoEM.
DOI: 10.15151/esrf-es-656089449
title: In situ nanotomography of the sintering of agglomerated ceramic powder

description: This proposal aims at analysing the sintering of agglomerated submicronic ceramic powder by in situ nanotomography. High temperature sintering is the main fabrication process of ceramics. It involves complex phenomena that are difficult to observe with conventional techniques. 3D imaging in the course of sintering has proved to be highly valuable for improving the understanding of sintering of metal and glass powders. More recently, during MA-4632 experiment, a micron-size ceramic powder has been 3D imaged throughout sintering at 1500°C, taking advantage of the resolutions and scan times available at ID16B-NA. In this following project, we will use the same procedure for in situ observation of agglomerated submicron zinc oxide powder compacts that exhibit inter-agglomerate pores. Quantitative analysis of 3D images will allow following the changes of these pores in the course of sintering, which play a key role in the properties of sintered ceramic parts.
DOI: 10.15151/esrf-es-642714813
title: Structural analysis of protein machineries using single particle cryo-EM

description: Structures of large macromolecular machineries were for long time not studied at atomic level as they were often too large for X-ray crystallography and as electron microscopy was not allowing good enough resolution. In the last decade, however, tremendous progress has been achieved in the field of single particle cryo electron microscopy (cryo-EM), which became the method of choice to structurally characterize such large protein complexes. The goal of this BAG is to determine structures of complex and often dynamic protein machineries including multi-subunit complexes, protein-nucleic acid complexes or membrane protein complexes using cryo-EM. The projects aim at determining structures of macromolecular machineries involved in energy conversion and cellular respiration, in nitrate and ammonium metabolism, in ribosome and ribosome-associated functions and in DNA damage repair and maintenance.
DOI: 10.15151/esrf-es-651254450
title: Structural Biology at EMBL Grenoble, IBS-CIBB and IAB

description: The proposals covers a broad range of structural biology projects related to pathogen biology, host-pathogen interactions, RNA biology and structure-based drug development that are carried out by PIs at EMBL Grenoble, IBS-CIBB and IAB. The proposers have long-standing experience in the use, as well as the development of beam lines for macromolecular crystallography and have participated in successive BAG applications over the years, mostly at the ESRF but also at other synchrotrons (e.g. Soleil, Petra III, Diamond, SLS).
DOI: 10.15151/esrf-es-689498289
title: IBS BAG

description: The IBS BAG currently includes 24 IBS teams and 4 external groups from CERMAV and iRTSV/CEA (Grenoble), CEA-Cadarache (St Paul lez Durance) and IRBA (Brétigny-sur-Orge). We study structure-function relationships of proteins emphasizing in human health, biotechnology and methodology. Most of the projects can be grouped in different topics as follows: host-pathogen interaction, immunology, new drug targets, fundamental cellular mechanisms, membrane proteins, intrinsically disordered proteins, biotechnological applications and methodology. Some of these projects use integrative approaches (X-ray crystallography, SAXS, NMR (and cryo-EM), together with other biophysical studies) with the aim to fully understand the complexity of the biological macromolecular systems on study. Some other teams are dedicated to serial crystallography and its developments, for which the new ESRF-EBS might be the perfect tool.
DOI: 10.15151/esrf-es-643607825
title: ITABAG: 3D structures of macromolecules related to human health

description: The ITABAG includes structural biologists from Universities, National Research Council and Hospital research centres in Italy. The laboratories apply various diffraction methods to study the structure-function relationships in various macromolecules. A unifying factor for the vast majority of the macromolecules under study is that they are related to human health, either directly, being human proteins involved in some disease, or indirectly, as proteins expressed by human pathogens and validated as potential pharmacological targets. Other projects investigate basic chemical processes, such as crystal growth and polymer association and formation of nanostructures.
DOI: 10.15151/esrf-es-644000484
title: Structural Biology in Marseille

description: The BAG groups 8 teams from 4 Marseille laboratories. Research themes deal with infection, health and biotechnology. For 81 projects within this proposal we foresee 11 MX and 2 SAXS shifts for the next 6 months. This is less of what we had asked for in previous years, given that data collection speed has largely increased and several projects are now being tackled by Cryo-EM. To be added that during the ESRF shutdown all the activities of the BAG have moved to Soleil and the moving back of activities to ESRF is affected by natural inertia. 2 shifts for 6 month at the BIOSAXS beamline, split up in two sessions, suit our needs. Two teams of the BAG combine structural biology with medicinal chemistry and beam time at MASSIF for large ligand-screening campaigns will mostly suit their research purposes. We are grateful to all ESRF staff for always being forthcoming with regard to scheduling, logistics and experiments, allowing the BAG to produce good Science in a comfortable setting.
DOI: 10.15151/esrf-es-657042074
title: BAG STRASBOURG-NANCY-DIJON

description: The members of the BAG are working on different projects, including proteins, nucleic acids and nucleic acid-protein complexes. The teams from Nancy work on structure-function relationship of glutathione transferases and RNA-protein complexes. A team from Dijon works on proteins involved in genetic disorders. The IBMC study RNAP proteins and tRNA precursors with partners in relation with the evolution of translation machinery and with human pathologies, ribozymes and RNA-protein complexes involved in the mitochondrial import. IGBMC (Strasbourg-Illkirch) teams are focused on nuclear receptors and complexes involving nuclear receptors and co-activators or co-repressors, transcription factor complexes, RNA polymerases, epigenetic molecular targets or cancer related proteins as well as large protein-nucleic acids complexes such as ribosomes.
DOI: 10.15151/esrf-es-661753199
title: IBS BAG

description: The IBS BAG currently includes 24 IBS teams and 4 external groups from CERMAV and iRTSV/CEA (Grenoble), CEA-Cadarache (St Paul lez Durance) and IRBA (Brétigny-sur-Orge). We study structure-function relationships of proteins emphasizing in human health, biotechnology and methodology. Most of the projects can be grouped in different topics as follows: host-pathogen interaction, immunology, new drug targets, fundamental cellular mechanisms, membrane proteins, intrinsically disordered proteins, biotechnological applications and methodology. Some of these projects use integrative approaches (X-ray crystallography, SAXS, NMR (and cryo-EM), together with other biophysical studies) with the aim to fully understand the complexity of the biological macromolecular systems on study. Some other teams are dedicated to serial crystallography and its developments, for which the new ESRF-EBS might be the perfect tool.
DOI: 10.15151/esrf-es-686694262
title: FInnish National Protein Crystallography Consortium

description: The Finnish BAG encompasses 25 groups active in crystallography in Finland. The projects vary widely and include membrane proteins such as membrane pyrophosphatases, and various protein complexes and receptors (growth factor receptors, integrins), signaling proteins such as kinases, other proteins involved in disease and antibiotics development (neuronal adhesion and myelin proteins, PP2A, ADP-ribosylation and biocatalytic enzymes) and several pathogen proteins (e.g. viral proteins) and various enzyme targets and e.g. studies on phytochrome photoreceptors and complexes involved in actin and cytoskeleton dynamics and regulation. Overall the BAG serves the national needs for highly variable projects, with different biological and biotechnological applications. Several project will benefit from microfocus beam lines and tunable wavelength options for phasing, others benefit from quick robust screening by MASSIF. Biology lab is needed for SAXS experiments.
DOI: 10.15151/esrf-es-656104687
title: Synchrotron Serial Crystallography (SSX) BAG

description: The aim of this BAG is the development of new methods, hardware and software for different applications in SSX. The new EBS machine is in the privileged position of exploiting flux density previously unmatched at synchrotron beamlines. This is likely to open a new paradigm in serial synchrotron crystallography, by enhancing the signal to noise of the diffraction data and reducing the minimum exposure time. The increase in photon flux density at the sample position will interest most of the MX beamlines and it is going to be particularly effective for microfocus beamline such as ID23-2 and ID30A3. We plan to further develop different SSX data collection methods in the attempt to profit of the characteristic of the new beam and to extend the implementation of automated procedures to simplify the access to SSX methods for the MX community.
DOI: 10.15151/esrf-es-656088651
title: Controlling chain entanglements in bottlebrush polymers for biomedical applications

description: Brush architecture disentangles network strands, increases osmotic pressure, and weakens the elastic force towards enhanced swellability. However, steric repulsion between side chains also leads to backbone strand extension resulting in increased non-linear stress response, which counteracts swelling. This tug-of-war governs the resulting mechanical properties of swollen gels and remains poorly understood. It is clear that brush side chains play multiple roles that may either promote or suppress gel swelling. In the present experiment, we will explore properties of bottlebrush-based elastomers upon exposure to various solvents. By performing in-situ USAXS/WAXS couples with fast mechanical stretching and heating of swollen samples we are planning to uncover the architecture-mediated interplay between gel assembly, swelling and mechanics. This knowledge will enable fabricating soft materials with orthogonal control of chemical composition, mechanical properties, and functionality.
DOI: 10.15151/esrf-es-656090746
title: Effect of volatile-containing glass beads on sintering evolution of lunar regolith simulants

description: The autonomous construction of shelters using in-situ resources, such as via additive manufacturing (3D printing) of regolith feedstock, is a necessary prerequisite and priority to sustain longer duration human presence on the Moon from both a cost and risk perspective. We aim to use powder diffraction data to generate the baseline fundamental description of simulants ‘TUBS-M’ and ‘TUBS-T’, with a particular emphasis on phase evolution during sintering and recrystallization. For improved fidelity we propose here to look at the expected strong influence of systematically incorporating two distinct volatile-containing glass beads types according to returned Apollo specimens to 1) characterise the state of the sample during the process as a function of glass content, 2) observe sintering rates as a function of the same, and 3) model sintering behaviour, supported by external mechanical testing.
DOI: 10.15151/esrf-es-642972022
title: Structural Biology of Macromolecules and Macromolecular complexes from India

description: Structural biology research groups located in India constitute the INDIA-BAG and will utilize MX, SAXS and CryoEM to study different biological macromolecules. Together, these groups address multiple pathways in animals, plants, bacteria and fungi. These studies will provide fundamental mechanistic insight regarding different processes critical for the survival and propagation of the relevant organism. Many groups in the BAG study proteins from pathogens to identify novel intervention points that can be the targeted with small molecule inhibitors to inhibit the growth of the corresponding infectious agents. There are more than 50 groups that are part of this BAG and the allocated beamtime will be available for over 500 young researchers. A brief description of all the research groups is provided in the global summary and a summary of the research contributions involving data collected at ESRF is provided in the last BAG report.
DOI: 10.15151/esrf-es-644086379
title: Structural studies of proteins and protein complexes involved in regulation, recognition and transport

description: We are a large BAG of research groups with varied interests and technical requirements, from routine rapid collection of diffraction data from well behaved systems for ligand studies to challenging microcrystals grown using cubic phase methods. Our BAG is focussed around a large group of experimenters who work on a diverse range of biological and physical problems. Whilst this makes it difficult to write an overall summary of the science it makes it easy to share the beamtime very efficiently and ensure that all time granted is used to the fullest extent.
DOI: 10.15151/esrf-es-649494318
title: Macromolecular Crystallography at South-East Andalusia

description: This BAG is a continuation of our previous proposals bringing together three main crystallography groups, UAL, UGR and CSIC. Thse groups agglutinate the crystallography needs of several other teams established through permanent collaborations. It is a continuation of previous BAGs: Mx1406/Mx1541, Mx1629/Mx1739, Mx1830/Mx1938, Mx2064 and Mx 2281(currently running). Our team and collaborators covers a wide range of biotechnological and biomedical topics including: i) the development of ancestral reconstructed enzymes; ii) deciphering the molecular basis for different human pathologies, such as protein miss-folding or protein signalling in innate immunity and inflammation diseases; iii) the determination of the molecular basis governing different biocatalysts of economic significance; iv) the discovery of novel chemotaxis processes exerted by previously unreported bacterial chemoreceptors and v) expansion of protein crystallization and protein crystal-derived methodologies.
DOI: 10.15151/esrf-es-658019718
title: Belgian BAG

description: The BAG includes groups situated at four Flemish universities: Antwerp, Brussels, Ghent and Leuven. Several of these groups are part of the elite Flemish Institute of Biotechnology (VIB). The proposed projects are highly diverse, including viral, prokaryotic and eukaryotic proteins with a strong focus on targets and processes of biomedical relevance. Many projects deal with membrane proteins, cell surface receptors and protein-protein complexes. Central to the research in the BAG associated groups is the employment of integrative methods in structural biology combining X-ray crystallography, SAXS, and cryo-electron microscopy. Many crystals in the various proposed projects are small in size and radiation sensitive, requiring the use of the high brilliance MX beam lines, preferably with micro-focused X-rays. This is a continuation of a previous Belgian BAG which has resulted in numerous top-tier publications.
DOI: 10.15151/esrf-es-649778060
title: Southampton, Bristol, Exeter, KCL, Portsmouth, UCL Royal Free Block Allocation Group (BAG)

description: This BAG coordinates activities of groups from the South-West of the UK. The focus is on projects in Immunology, transcriptional regulation, and enzymology. A particular strength are the macromolecular complexes that several of the groups target. The activities in rational protein design (Bristol) and enzyme design (Portsmouth) are particular highlight and have enriched the portfolio of projects of this ag since joining in 2020.
DOI: 10.15151/esrf-es-708311580
title: Despite the odds: formation of the SARS-CoV-2 methylation complex (rapid access Covid-19 project)

description: Coronaviruses protect their ssRNA genome with a methylated cap. The methylation is performed by two methyltransferases, nsp14 and nsp16. Additionally, nsp14 carries an exonuclease domain, which operates in the proofreading system. nsp14 and nsp16 were reported to independently bind nsp10, but the available structural information suggests that the concomitant interaction between these three proteins should be impossible due to steric clashes. In our work (https://www.biorxiv.org/content/10.1101/2022.01.25.477673v1 ), we show that nsp14, nsp10, and nsp16 can form a ternary complex (MST, enzymatic assays, SAXS, TEM). This interaction is expected to encourage formation of mature capped viral mRNA, modulating the nsp14 exonuclease activity, and protecting the viral RNA. A high-resolution structure of the triplex would greatly improve the understanding of how the component proteins are undergoing the structural changes upon the ternary complex formation.
DOI: 10.15151/esrf-es-657037634
title: In-situ compression of Mg-based AM scaffolds for biomedical applications

description: Laser Additive Manufacturing (AM) of magnesium is extremely challenging, and only recently, it became possible to 3D print scaffolds of Mg-alloys. Mg-alloys are attractive for orthopedic application due to their biocompatibility and mechanical properties. However Mg-alloys suffer rapid biodegradation. The mechanical and biodegradation properties of these biomaterials are extremely important for their proper functioning, because the human body behaves as a corrosive environment with complex cyclic loading, which can cause mechanical failure of implants. In this context, AM biomaterials can be designed to adjust their properties. We aim at carrying out in-situ compression tests during tomography of AM scaffolds (before and after controlled degradation) to assess crack initiation and propagation mechanisms and their interrelation with the degradation behavior. The tomographic information will be used to feed numerical models of mechanical response and the degradation behavior combined.
DOI: 10.15151/esrf-es-642972193
title: Potential induced restructuring of copper electrodes: stability and site specificity for CO2 reduction

description: Electroreduction of CO2 represents a promising approach towards artificial carbon recycling for addressing global challenges in energy and sustainability. The product selectivity during CO2 reduction on single crystal electrodes is associated to the adsorbed species and composition of the electrochemical interphase. On Cu(001) adsorption of oxygenated species leads to faceting of the surface. At potentials where no oxygenated species is adsorbed,a change in the faceting was observed. We aim to study the time evolution of the restructuring on the Cu(001) surface in the presence of an inert gas, oxygen and CO2 with High-Energy Surface X-ray diffraction. The technique is essential to follow the restructuring process on the relevant time scale. The results will provide valuable understanding. of the role of the oxides and oxide reaction process in the electrochemical reduction of CO2 on copper and copper oxides which will be crucial in the development of active and selective catalysts.
DOI: 10.15151/esrf-es-656089266
title: Inderite and inderborite at non-ambient conditions

description: Among hydrated borates, inderite and inderborite are two mineralogical species which display a different H2O content (40 wt% in inderborite and 48 wt% in inderite, respectively). In the last years, our team have studied several hydrated borates, each one displaying one (or more) phase transition at high-pressure in the P-range 1.6-14 GPa. The findings suggest a linear correlation between the H2O content and the pressure at which a hydrated borate undergoes a phase transition, but more studies are needed in order to confirm a real trend. Furthermore, hydrated borates are believed to be a potential aggregate in radiation-shielding concretes due to the large cross section for thermal neutron of the isotope 10B. A comprehensive characterization of the crystal-chemistry, elastic properties, stability and structural behavior of natural borates at varying T and P conditions is advisable for modelling their behavior as aggregates in radiation-shielding concretes.
DOI: 10.15151/esrf-es-656105884
title: High-resolution RIXS study of the relation between acoustic plasmons and superconductivity in cuprates

description: Despite more than 30 years of intense research on high-Tc superconducting cuprates, a comprehensive understanding of the mechanisms that lead to their exceptionally strong superconductivity has remained elusive. Using Cu L3-edge resonant inelastic x-ray scattering (RIXS), three-dimensional collective charge excitations were revealed in electron-doped cuprates, which subsequently were also observed in hole-doped cuprates by O K-edge RIXS. Interestingly, these collective excitations correspond to the long-anticipated acoustic plasmon modes of cuprates, which were suggested to contribute to the mediation of superconducting pairing, and their evolution across Tc could reflect a possible saving of kinetic energy correlated with the superconducting transition. Here we propose an O K-edge RIXS study on the hole-doped cuprate YBa2Cu3O7 to investigate the behavior of acoustic plasmons above and below the superconducting transition and a possible relation to the elevated Tc of cuprates.