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5. EasyGrid: A new automated cryo-multimodal sample preparation

Author

Bissardon Caroline, Armijo Victor, Gemin Olivier, Felisaz Franck, Sinoir Jérémy, Felisaz Arthur, Deckers Thibault, Lecomte Léa, Cohen Raphael, Rossi Christopher, Janocha Robert, Lauzier Kevin, Linares Romain, Hons Michael, Schneider Sarah, Bowler Matthew W., Cloetens Peter, Galej Wojciech, Mahamid Julia, Eustermann Sebastian, Mattei Simone, Cipriani Florent, and Papp Gergely

Subjects
electronmicroscopy, x-rayfluorescence (xrf), single-particleanalysis, cryo-samplepreparation, Microbiology, QR1-502, Physiology, QP1-981, Zoology, QL1-991
Published
2024
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8. EasyGrid: a versatile platform for automated cryo-EM sample preparation and quality control

Author

Gemin, Olivier, primary, Armijo, Victor, additional, Hons, Michael, additional, Bissardon, Caroline, additional, Linares, Romain, additional, Bowler, Matthew W., additional, Wolff, Georg, additional, Kovalev, Kirill, additional, Babenko, Anastasiia, additional, Salo, Veijo T., additional, Schneider, Sarah, additional, Rossi, Christopher, additional, Lecomte, Léa, additional, Deckers, Thibault, additional, Lauzier, Kévin, additional, Janocha, Robert, additional, Felisaz, Franck, additional, Sinoir, Jérémy, additional, Galej, Wojciech, additional, Mahamid, Julia, additional, Müller, Christoph W., additional, Eustermann, Sebastian, additional, Mattei, Simone, additional, Cipriani, Florent, additional, and Papp, Gergely, additional

Published
2024
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13. A duplex structure of SARM1 octamers stabilized by a new inhibitor

Author

Khazma, Tami, primary, Golan-Vaishenker, Yarden, additional, Guez-Haddad, Julia, additional, Grossman, Atira, additional, Sain, Radhika, additional, Weitman, Michal, additional, Plotnikov, Alexander, additional, Zalk, Ran, additional, Hons, Michael, additional, and Opatowsky, Yarden, additional

Published
2022
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17. Structure of the human heparan sulfate polymerase complex EXT1-EXT2

Author

Leisico, Francisco, primary, Omeiri, Juneina, additional, Le Narvor, Christine, additional, Beaudouin, Joёl, additional, Hons, Michael, additional, Fenel, Daphna, additional, Schoehn, Guy, additional, Couté, Yohann, additional, Bonnaffé, David, additional, Sadir, Rabia, additional, Lortat-Jacob, Hugues, additional, and Wild, Rebekka, additional

Published
2022
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18. A Duplex Structure of SARM1 Octamers Induced by a New Inhibitor

Author

Khazma, Tami, primary, Golan-Vaishenker, Yarden, additional, Guez-Haddad, Julia, additional, Grossman, Atira, additional, Sain, Radhika, additional, Plotnikov, Alexander, additional, Zalk, Ran, additional, Yaron, Avraham, additional, Hons, Michael, additional, and Opatowsky, Yarden, additional

Published
2022
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19. Assembly of The Mitochondrial Complex I Assembly Complex Suggests a Regulatory Role for Deflavination

Author

Giachin, Gabriele, Jessop, Matthew, Bouverot, Romain, Acajjaoui, Samira, Saïdi, Melissa, Chretien, Anaïs, Bacia‐Verloop, Maria, Signor, Luca, Mas, Philippe J., Favier, Adrien, Borel Meneroud, Eve, Hons, Michael, Hart, Darren J., Kandiah, Eaazhisai, Boeri Erba, Elisabetta, Buisson, Alain, Leonard, Gordon, Gutsche, Irina, Soler‐Lopez, Montserrat, European Synchrotron Radiation Facility (ESRF), Institut de biologie structurale (IBS - UMR 5075), Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes (UGA), Inserm, U1216, Grenoble, France., Institut National de la Santé et de la Recherche Médicale (INSERM), European Molecular Biology Laboratory [Grenoble] (EMBL), ISBG, ANR-10-INBS-0005,FRISBI,Infrastructure Française pour la Biologie Structurale Intégrée(2010), ANR-10-LABX-0049,GRAL,Grenoble Alliance for Integrated Structural Cell Biology(2010), ANR-17-EURE-0003,CBH-EUR-GS,CBH-EUR-GS(2017), European Project: grant number 647784, Thomas, Frank, Infrastructure Française pour la Biologie Structurale Intégrée - - FRISBI2010 - ANR-10-INBS-0005 - INBS - VALID, Grenoble Alliance for Integrated Structural Cell Biology - - GRAL2010 - ANR-10-LABX-0049 - LABX - VALID, CBH-EUR-GS - - CBH-EUR-GS2017 - ANR-17-EURE-0003 - EURE - VALID, and European Union’s Horizon 2020 - grant number 647784 - INCOMING

Subjects
[SDV.BBM.BS] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], ACAD9, deflavination, Oxidative Phosphorylation, 03 medical and health sciences, Acyl-CoA Dehydrogenases, mitochondrial complex I assembly complex, Humans, Protein Interaction Domains and Motifs, Cryo-EM, FAD, Research Articles, Adaptor Proteins, Signal Transducing, 030304 developmental biology, 0303 health sciences, Electron Transport Complex I, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], Cryoelectron Microscopy, 030302 biochemistry & molecular biology, General Medicine, Recombinant Proteins, Mitochondria, Protein Structure, Tertiary, Flavin-Adenine Dinucleotide, Mitochondrial Pathways, Energy Metabolism, Research Article
Abstract

Fatty acid β‐oxidation (FAO) and oxidative phosphorylation (OXPHOS) are mitochondrial redox processes that generate ATP. The biogenesis of the respiratory Complex I, a 1 MDa multiprotein complex that is responsible for initiating OXPHOS, is mediated by assembly factors including the mitochondrial complex I assembly (MCIA) complex. However, the organisation and the role of the MCIA complex are still unclear. Here we show that ECSIT functions as the bridging node of the MCIA core complex. Furthermore, cryo‐electron microscopy together with biochemical and biophysical experiments reveal that the C‐terminal domain of ECSIT directly binds to the vestigial dehydrogenase domain of the FAO enzyme ACAD9 and induces its deflavination, switching ACAD9 from its role in FAO to an MCIA factor. These findings provide the structural basis for the MCIA complex architecture and suggest a unique molecular mechanism for coordinating the regulation of the FAO and OXPHOS pathways to ensure an efficient energy production., Fatty acid oxidation (FAO) and oxidative phosphorylation (OXPHOS) are key mitochondrial pathways for cellular energetics. However, the crosstalk between them is unclear. We show that the molecular architecture of the mitochondrial Complex I assembly (MCIA) complex, required for Complex I biogenesis and thereby for activation of OXPHOS, implies an allosteric deflavination mechanism that shuts down FAO.

Published
2020

20. Structural basis for SARM1 inhibition and activation under energetic stress

Author

Sporny, Michael, Guez-Haddad, Julia, Khazma, Tami, Yaron, Avraham, Dessau, Moshe, Shkolnisky, Yoel, Mim, Carsten, Isupov, Michail N., Zalk, Ran, Hons, Michael, Opatowsky, Yarden, Sporny, Michael, Guez-Haddad, Julia, Khazma, Tami, Yaron, Avraham, Dessau, Moshe, Shkolnisky, Yoel, Mim, Carsten, Isupov, Michail N., Zalk, Ran, Hons, Michael, and Opatowsky, Yarden

Abstract

SARM1, an executor of axonal degeneration, displays NADase activity that depletes the key cellular metabolite, NAD+, in response to nerve injury. The basis of SARM1 inhibition and its activation under stress conditions are still unknown. Here, we present cryo-EM maps of SARM1 at 2.9 and 2.7 angstrom resolutions. These indicate that SARM1 homo-octamer avoids premature activation by assuming a packed conformation, with ordered inner and peripheral rings, that prevents dimerization and activation of the catalytic domains. This inactive conformation is stabilized by binding of SARM1's own substrate NAD+ in an allosteric location, away from the catalytic sites. This model was validated by mutagenesis of the allosteric site, which led to constitutively active SARM1. We propose that the reduction of cellular NAD+ concentration contributes to the disassembly of SARM1's peripheral ring, which allows formation of active NADase domain dimers, thereby further depleting NAD+ to cause an energetic catastrophe and cell death., QC 20210107

Published
2020
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21. Assembly of The Mitochondrial Complex I Assembly Complex Suggests a Regulatory Role for Deflavination

Author

Giachin, Gabriele, primary, Jessop, Matthew, additional, Bouverot, Romain, additional, Acajjaoui, Samira, additional, Saïdi, Melissa, additional, Chretien, Anaïs, additional, Bacia‐Verloop, Maria, additional, Signor, Luca, additional, Mas, Philippe J., additional, Favier, Adrien, additional, Borel Meneroud, Eve, additional, Hons, Michael, additional, Hart, Darren J., additional, Kandiah, Eaazhisai, additional, Boeri Erba, Elisabetta, additional, Buisson, Alain, additional, Leonard, Gordon, additional, Gutsche, Irina, additional, and Soler‐Lopez, Montserrat, additional

Published
2021
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26. Automated Surveillance of Subsurface Wellbore Integrity in a Heavy Oil Field using Passive Seismic Systems

Author

Simona Costin, Yam Helen, Jeffrey R. Bailey, Hayward Tim W, Colin Brisco, Lolla Sri Venkata Tapovan, Liu Xinlong, Hons Michael S, and Akhmetov Arslan

Subjects
Wellbore, Microseism, Petroleum engineering, Passive seismic, Oil field, Geology
Abstract

Continuous subsurface surveillance is important for heavy oil in-situ recovery processes where induced stresses in the overburden can compromise the integrity of the wellbores. Wellbore failure may lead to the undesirable loss of fluids into the overburden. In recent years, there has been a rapid growth in the use of Passive Seismic monitoring systems to aid in subsurface surveillance activities, with the ultimate goal of detecting potential integrity issues as early as possible. However, the massive volume of data recorded by these instruments is time-consuming and error-prone to process manually. This paper introduces EMMAA (ExxonMobil Microseismic Automated Analyzer), an automated workflow to reliably process continuous microseismic data, detect subsurface integrity issues, and ultimately reduce the latency in responding to wellbore integrity issues. A novel cloud-based technology for managing microseismic data is briefly described. The seismic waveforms, recorded by a distributed array of geophone receivers, are automatically analyzed to determine the type and source of subsurface disturbances (‘events’). First, novel frequency-domain and deep learning analyses are used to distinguish noisy signals from the seismic waveforms such as compressional and shear waves produced by the events. Next, the location of the event is calculated and its seismic attributes are computed. Finally, the type and severity of the seismic event are determined by an event classifier. The performance of the automated workflow is examined in the context of accurate detection of casing failures in a heavy oil Cyclic Steam Stimulation (CSS) application. The event features that distinguish casing breaks from other seismic events are described. It is shown that the methodology is able to achieve a high detection rate when back-tested against a historical data-set of known casing failures. False positives are adequately contained by preventing waveforms of electrical or mechanical noise from being processed. In a production environment, the event processing workflow is run on distributed servers and analyzes triggered seismic data in real-time. Depending on the severity of the microseismic events detected, operators are immediately alerted via email and text messages, so that remedial actions may be swiftly initiated. The utility of this integrated system is further exemplified by the massive reduction in the time taken to detect casing breaks—from up to 36 hours historically, down to less than one hour in most instances. Extensions of EMMAA that enable the detection of a wide variety of microseismic events are also discussed. These events include surface casing slips that occur at the casing shoe, cement de-bonding events near the wellbores, and events indicative of potential fluid migration in the overburden.

Published
2019

27. CM01: a facility for cryo-electron microscopy at the European Synchrotron

Author

Kandiah, Eaazhisai, Giraud, Thierry, de Maria Antolinos, Alejandro, Dobias, Fabien, Effantin, Gregory, Flot, David, Hons, Michael, Schoehn, Guy, Susini, Jean, Svensson, Olof, Leonard, Gordon A., Mueller-Dieckmann, Christoph, European Synchrotron Radiation Facility (ESRF), Institut de biologie structurale (IBS - UMR 5075 ), Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), and Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)

Subjects
[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], Macromolecular Substances, X-Rays, CM01, cryo-TEM, education, Cryoelectron Microscopy, macromolecular substances, urologic and male genital diseases, Feature Articles, Tobacco Mosaic Virus, PSB, cryo-EM platform, Tobacco, ESRF, France, Software, Synchrotrons
Abstract

CM01 is a recently opened cryo-electron microscopy facility located at the European Synchrotron and is used by the ESRF’s international community for structural biology., Recent improvements in direct electron detectors, microscope technology and software provided the stimulus for a ‘quantum leap’ in the application of cryo-electron microscopy in structural biology, and many national and international centres have since been created in order to exploit this. Here, a new facility for cryo-electron microscopy focused on single-particle reconstruction of biological macromolecules that has been commissioned at the European Synchrotron Radiation Facility (ESRF) is presented. The facility is operated by a consortium of institutes co-located on the European Photon and Neutron Campus and is managed in a similar fashion to a synchrotron X-ray beamline. It has been open to the ESRF structural biology user community since November 2017 and will remain open during the 2019 ESRF–EBS shutdown.

Published
2019

30. 3D structure of the natural tetrameric form of human butyrylcholinesterase as revealed by cryoEM, SAXS and MD

Author

Boyko, Konstantin M., primary, Baymukhametov, Timur N., additional, Chesnokov, Yury M., additional, Hons, Michael, additional, Lushchekina, Sofya V., additional, Konarev, Petr V., additional, Lipkin, Alexey V., additional, Vasiliev, Alexandre L., additional, Masson, Patrick, additional, Popov, Vladimir O., additional, and Kovalchuk, Michail V., additional

Published
2019
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38. 3D STRUCTURE OF NATURAL TETRAMERIC FORM OF HUMAN BUTYRYLCHOLINESTERASE OBTAINED BY CRYO-ELECTRON MICROSCOPY.

Author

Boyko, Konstantin M., Baimukhametov, Timur N., Chesnokov, Yury M., Hons, Michael, Lushchekina, Sofya V., Konarev, Peter, Lipkin, Alexey, Vasiliev, Alexandre L., Masson, Patrick, and Popov, Vladimir

Subjects
BUTYRYLCHOLINESTERASE, CRYOELECTRONICS, CHOLINESTERASE reactivators, ATOMIC structure, ELECTRON density
Abstract

Human butyrylcholinesterase (BChE) is a stoichiometric bioscavenger of toxic organophosphates. It can be used as an antidote to protect acetylcholinesterase, and is a protein of choice for development of detoxification biocatalysts for clinical applications. Despite the number of different monomeric structures of recombinant human BChE obtained to date, all attempts to obtain an atomic structure of the natural glycosylated tetrameric BChE were unsuccessful. Here, we present for the first time the 3D structure of the natural tetrameric form of human butyrylcholinesterase, obtained by Cryo-EM technique at a final resolution of 8.8Å. The tetramer has a C2 symmetry, with all subunits arranged as a "propeller-like" tetramer. This is in contrast with previous "flat" model of subunits arrangement in tetramer. Cryo-EM structure shows that the two opposite BChE subunits are placed higher (or lower) the plane of the other two subunits. Despite glycan chains were obscured in the electron density due to their relative disoder, they could be modeled based on the positions of the residues anchoring these glycans. The electron density allowed to distinguish that C-terminal tails of all the subunits interact with each other and form a helix around the PRADpeptide, supporting rigidity of the tail. The tail is situated in the center of the tetramer and is oriented nearly perpendicular to the tetramer "plane".It was also observed that the subunits in the tetramer have different contacts with neighbouring subunits. This allows to consider the tetramer as a dimer of dimers which is additionally strengthened by the C-terminal tail interactions. [ABSTRACT FROM AUTHOR]

Published
2018

39. Relationship of Physical Characteristics, Personality Traits, and Biographical Data to Success of Flight Attendants

Author

Hons, Michael Jerome

Subjects
job success, Flight attendants -- Selection and appointment, Prediction of occupational success, job performance, biographical data, flight attendants
Abstract

With the EEOC requiring empirical criterion-related validity for selection procedures, predictor variables of physical characteristics, biographical data, and personality traits were related to both on-the-job performance and training performance. In the correlational analysis of the variables, a total of 455 flight attendants from a single airline were used, with half of the subjects serving as a cross-validation sample. The results showed slight relationships between biographical data and physical characteristics to training performance but no relationship between any predictor variable and job performance. The impact of race being a significant predictor of training performance was reviewed. The lack of practical information was discussed, and implications made for future research to include proper design and reliability of screening procedures before attempting criterion-related validation.

Published
1980

40. CM01: a facility for cryo-electron microscopy at the European Synchrotron.

Author

Kandiah E, Giraud T, de Maria Antolinos A, Dobias F, Effantin G, Flot D, Hons M, Schoehn G, Susini J, Svensson O, Leonard GA, and Mueller-Dieckmann C

Subjects
France, Nicotiana virology, X-Rays, Cryoelectron Microscopy methods, Macromolecular Substances ultrastructure, Software, Synchrotrons instrumentation, Tobacco Mosaic Virus ultrastructure
Abstract

Recent improvements in direct electron detectors, microscope technology and software provided the stimulus for a `quantum leap' in the application of cryo-electron microscopy in structural biology, and many national and international centres have since been created in order to exploit this. Here, a new facility for cryo-electron microscopy focused on single-particle reconstruction of biological macromolecules that has been commissioned at the European Synchrotron Radiation Facility (ESRF) is presented. The facility is operated by a consortium of institutes co-located on the European Photon and Neutron Campus and is managed in a similar fashion to a synchrotron X-ray beamline. It has been open to the ESRF structural biology user community since November 2017 and will remain open during the 2019 ESRF-EBS shutdown., (open access.)

Published
2019
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