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1. The Structure Function Ratios F2(Li)/F2(D) and F2(C)/F2(D) at small x

Author

THE NEW MUON COLLABORATION, Arneodo, M., Arvidson, A., Badelek, B., Ballintijn, M., Baum, G., Beaufays, J., Bird, I. G., Bjorkholm, P., Botje, M., Broggini, C., Bruckner, W., Brull, A., Burger, W. J., Ciborowski, J., van~Dantzig, R., Dyring, A., Engelien, H., Ferrero, M. I., Fluri, L., Gaul, U., Granier, T., Grosse-Perdekamp, M., von~Harrach, D., van~der~Heijden, M., Heusch, C., Igo, G., Ingram, Q., Janson-Prytz, K., de~Jong, M., Kabuss, E. M., Kaiser, R., Kessler, H. J., Ketel, T. J., Klein, F., Kullander, S., Landgraf, U., Lindqvist, T., Mallot, G. K., Mariotti, C., van~Middelkoop, G., Milsztajn, A., Mizuno, Y., Most, A., Mucklich, A., Nassalski, J., Nowotny, D., Oberski, J., Paic, A., Peroni, C., Povh, B., Rieger, R., Rith, K., Rohrich, K., Rondio, E., Ropelewski, L., Sandacz, A., Sanders, D., Scholz, C., Seitz, R., Sever, F., Shibata, T. -A., Siebler, M., Simon, A., Staiano, A., Szleper, M., Tzamouranis, Y., Virchaux, M., Vuilleumier, J. L., Walcher, T., Whitten, C., Windmolders, R., Witzmann, A., and Zetsche, F.

Subjects
High Energy Physics - Experiment
Abstract

We present the structure function ratios F2(Li)/F2(D) and F2(C)/F2(D) measured in deep inelastic muon-nucleus scattering at a nominal incident muon energy of 200 GeV. The kinematic range 0.0001 < x < 0.7 and 0.01< Q^2 < 70 GeV^2 is covered. For values of $x$ less than $0.002$ both ratios indicate saturation of shadowing at values compatible with photoabsorption results.

Published
1995
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4. Prompt fission product yields in the $^{238}$U(n,f) reaction

Author

Fotiades, N., Casoli, P., Jaffke, P., Devlin, M., Nelson R, O., Granier, T., Talou, P., Ethvignot, T., CADARACHE, Bibliothèque, Los Alamos National Laboratory (LANL), CEA-Direction des Energies (ex-Direction de l'Energie Nucléaire) (CEA-DES (ex-DEN)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Autorié de sureté nucléaire (ASN), and Direction des Applications Militaires (DAM)

Subjects
[PHYS.NUCL] Physics [physics]/Nuclear Theory [nucl-th], Yields, [PHYS.NUCL]Physics [physics]/Nuclear Theory [nucl-th], Fission Fragments, [PHYS.NEXP] Physics [physics]/Nuclear Experiment [nucl-ex], Uranium 238, [PHYS.NEXP]Physics [physics]/Nuclear Experiment [nucl-ex]
Abstract

International audience; Background: Significant yield discrepancies (500%–600%) were reported recently between experimentalresults and predictions (from the GEF model) and evaluations (from the JEFF-3.1.1 and ENDF/B-VII.1 libraries)for Mo and Sn fission-fragment yields in fast-neutron-induced reactions on $^{238}$U using $\gamma$ -$\gamma$ -$\gamma$ coincidence spectroscopy. The model and evaluations also predict Mo and Sn fragments that are on average $\sim$1 to 2 neutrons richer than the experimental results.Purpose: $\gamma$ -$\gamma$ -$\gamma$ coincidence spectroscopy favors detection of higher-multiplicity γ -ray cascades. An alternative approach is determining the fragment yields using single-$\gamma$-ray spectroscopy, as it was attempted here for selected cases where it was feasible. Advantages and drawbacks in both approaches need to be understood and potential systematic errors in the experimental results should be addressed using theoretical models. Methods: Fast neutrons from the LANSCE WNR facility were used to induce fission on $^{238}$U. The emitted γrays were measured with the GEANIE spectrometer.Results: The yield of selected even-even fission fragments was determined. The selection was based on theability to reliably determine excitation functions for the detected γ rays.Conclusions: Our single-γ -ray results provide better agreement between experiment and predictions andevaluations.

Published
2019

5. Report on the detection and acquisition systems at NFS

Author

Ledoux, X., Eric Bauge, Belier, G., Caillaud, T., Chatillon, A., Granier, T., Landoas, O., Taïeb, J., Rossé, B., Thfoin, I., Varignon, C., Blideanu, V., Doré, D., Gunsing, F., Panebianco, S., Ridikas, D., Takibayev, A., Aïche, M., Barreau, G., Czajkowski, S., Jurado, B., Ban, G., Lecolley, F. R., Lecolley, J. F., Lecouey, J. L., Nathalie Marie, Steckmeyer, J. C., Dessagne, P., Kerveno, M., Rudolf, G., Bem, P., Majerle, M., Mrazek, J., Novak, J., Simeckova, E., Gustavsson, C., Pomp, S., Fischer, U., Klix, K., Simakov, S. P., Jacquot, B., Farget, F., Wieleczko, J. P., Perrot, L., Tassan-Got, L., Avrigeanu, M., Avrigeanu, V., Borcea, C., Negoita, F., Petrascu, M., Oberstedt, S., Plompen, A. J. M., Muriel Fallot, Lydie Giot, Smith, G., Tsekhanovich, I., Olivier Serot, Balanzat, E., Ban-D État, B., Guillous, S., Ramillon, J. M., Oberstedt, A., Sublet, J. C., DAM Île-de-France (DAM/DIF), Direction des Applications Militaires (DAM), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Institut de Recherches sur les lois Fondamentales de l'Univers (IRFU), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay, Aval du cycle et Energie Nucléaire (ACEN), Centre d'Etudes Nucléaires de Bordeaux Gradignan (CENBG), Université Sciences et Technologies - Bordeaux 1 (UB)-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Centre National de la Recherche Scientifique (CNRS)-Université Sciences et Technologies - Bordeaux 1 (UB)-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Centre National de la Recherche Scientifique (CNRS), Laboratoire de physique corpusculaire de Caen (LPCC), Université de Caen Normandie (UNICAEN), Normandie Université (NU)-Normandie Université (NU)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Centre National de la Recherche Scientifique (CNRS), Institut Pluridisciplinaire Hubert Curien (IPHC), Université de Strasbourg (UNISTRA)-Université de Haute-Alsace (UHA) Mulhouse - Colmar (Université de Haute-Alsace (UHA))-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Centre National de la Recherche Scientifique (CNRS), Grand Accélérateur National d'Ions Lourds (GANIL), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Centre National de la Recherche Scientifique (CNRS), Institut de Physique Nucléaire d'Orsay (IPNO), Université Paris-Sud - Paris 11 (UP11)-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Centre National de la Recherche Scientifique (CNRS), Laboratoire SUBATECH Nantes (SUBATECH), Mines Nantes (Mines Nantes)-Université de Nantes (UN)-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Centre National de la Recherche Scientifique (CNRS), CEA-Direction des Energies (ex-Direction de l'Energie Nucléaire) (CEA-DES (ex-DEN)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Centre de recherche sur les Ions, les MAtériaux et la Photonique (CIMAP - UMR 6252), Normandie Université (NU)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche sur les Matériaux Avancés (IRMA), Normandie Université (NU)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université de Rouen Normandie (UNIROUEN), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Centre National de la Recherche Scientifique (CNRS), Université Sciences et Technologies - Bordeaux 1-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Centre National de la Recherche Scientifique (CNRS)-Université Sciences et Technologies - Bordeaux 1-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Centre National de la Recherche Scientifique (CNRS), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3), Université de Strasbourg (UNISTRA)-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3), Centre National de la Recherche Scientifique (CNRS)-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Université Paris-Sud - Paris 11 (UP11), Centre National de la Recherche Scientifique (CNRS)-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Université de Nantes (UN)-Mines Nantes (Mines Nantes), Centre National de la Recherche Scientifique (CNRS)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Normandie Université (NU)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université de Caen Normandie (UNICAEN), and Normandie Université (NU)

Subjects
[PHYS.PHYS.PHYS-INS-DET]Physics [physics]/Physics [physics]/Instrumentation and Detectors [physics.ins-det], [PHYS.NEXP]Physics [physics]/Nuclear Experiment [nucl-ex]
Published
2012

6. The Neutrons for Science Facility at SPIRAL-2

Author

Ledoux, X., Aiche, M., Avrigeanu, M., Avrigeanu, V., Audouin, L., Balanzat, E., Ban-detat, B., Ban, G., Barreau, G., Bauge, E., Belier, G., Bem, P., Blideanu, V., Borcea, C., Bouffard, S., Caillaud, T., Chatillon, A., Czajkowski, S., Dessagne, P., Dore, D., Fallot, M., Farget, F., Fischer, U., Giot, L., Granier, T., Guillous, S., Gunsing, F., Gustavsson, Cecilia, Jacquot, B., Jansson, Kaj, Jurado, B., Kerveno, M., Klix, A., Landoas, O., Lecolley, F. R., Lecouey, J. L., Majerle, M., Marie, N., Materna, T., Mrazek, J., Negoita, F., Novak, J., Oberstedt, S., Oberstedt, A., Panebianco, S., Perrot, L., Plompen, A. J. M., Pomp, Stephan, Ramillon, J. M., Ridikas, D., Rosse, B., Rudolf, G., Serot, O., Simakov, S. P., Simeckova, E., Smith, A. G., Sublet, J. C., Taieb, J., Tassan-Got, L., Tarrio, D., Takibayev, A., Thfoin, I., Tsekhanovich, I., Varignon, C., Ledoux, X., Aiche, M., Avrigeanu, M., Avrigeanu, V., Audouin, L., Balanzat, E., Ban-detat, B., Ban, G., Barreau, G., Bauge, E., Belier, G., Bem, P., Blideanu, V., Borcea, C., Bouffard, S., Caillaud, T., Chatillon, A., Czajkowski, S., Dessagne, P., Dore, D., Fallot, M., Farget, F., Fischer, U., Giot, L., Granier, T., Guillous, S., Gunsing, F., Gustavsson, Cecilia, Jacquot, B., Jansson, Kaj, Jurado, B., Kerveno, M., Klix, A., Landoas, O., Lecolley, F. R., Lecouey, J. L., Majerle, M., Marie, N., Materna, T., Mrazek, J., Negoita, F., Novak, J., Oberstedt, S., Oberstedt, A., Panebianco, S., Perrot, L., Plompen, A. J. M., Pomp, Stephan, Ramillon, J. M., Ridikas, D., Rosse, B., Rudolf, G., Serot, O., Simakov, S. P., Simeckova, E., Smith, A. G., Sublet, J. C., Taieb, J., Tassan-Got, L., Tarrio, D., Takibayev, A., Thfoin, I., Tsekhanovich, I., and Varignon, C.

Abstract

The Neutrons For Science (NFS) facility is a component of SPIRAL-2 laboratory under construction at Caen (France). SPIRAL-2 is dedicated to the production of high intensity Radioactive Ions Beams (RIB). It is based on a high-power linear accelerator (LINAG) to accelerate deuterons beams in order to produce neutrons by breakup reactions on a C converter. These neutrons will induce fission in U-238 for production of radioactive isotopes. Additionally to the RIB production, the proton and deuteron beams delivered by the accelerator will be used in the NFS facility. NFS is composed of a pulsed neutron beam and irradiation stations for cross-section measurements and material studies. The beams delivered by the LINAG will allow producing intense neutron beams in the 100 keV-40 MeV energy range with either a continuous or quasi-mono-energetic spectrum. At NFS available average fluxes will be up to 2 orders of magnitude higher than those of other existing time-of-flight facilities in the 1 MeV - 40 MeV range. NFS will be a very powerful tool for fundamental physics and application related research in support of the transmutation of nuclear waste, design of future fission and fusion reactors, nuclear medicine or test and development of new detectors. The facility and its characteristics are described, and several examples of the first potential experiments are presented.

Published
2014
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7. The Electron-Ion Scattering experiment ELISe at the International Facility for Antiproton and Ion Research (FAIR) – a conceptual design study

Author

Antonov, A. N., Gaidarov, M. K., Ivanov, M. V., Kadrev, D. N., Aïche, M., Barreau, G., Czajkowski, S., Jurado, B., Belier, G., Chatillon, A., Granier, T., Taieb, J., Doré, D., Letourneaux, A., Ridikas, D., Dupont, E., Berthoumieux, E., Panebianco, S., Reymund, F., Schmitt, C., Audouin, L., Khan, E., Tassan-Got, L., Aumann, T., Beller, P., Boretzky, K., Dolinskii, A., Egelhof, P., Emling, H., Franzke, B., Geissel, H., Kelic-Heil, A., Kester, O., Kurz, N., Litvinov, Y., Münzenberg, G., Nolden, F., Schmidt, K.-H., Simon, H., Steck, M., Weick, H., Enders, J., Pietralla, N., Richter, A., Schrieder, G., Zilges, A., Distler, M. O., Merkel, H., Müller, U., Junghans, A., Lenske, H., Fujiwara, M., Suda, T., Kato, S., Adachi, T., Hamieh, S., Harakeh, M. N., Kalantar-Nayestanaki, N., Wörtche, H., Berg, G. P. A., Koop, I. A., Logatchov, P. V., Otboev, A. V., Parkhomchuk, V. V., Shatilov, D. N., Shatunov, P. Y., Shatunov, Y. M., Shiyankov, S. V., Shvartz, D. I., Skrinsky, A. N., Chulkov, L. V., Danilin, B. V., Korsheninnikov, A. A., Kuzmin, E. A., Ogloblin, A. A., Volkov, V. A., Grishkin, Y., Lisin, V. P., Mushkarenkov, A. N., Nedorezov, V., Polonski, A. L., Rudnev, N. V., Turinge, A. A., Artukh, A., Ershov, S. N., Fomichev, A., Golovkov, M., Gorshkov, A. V., Grigorenko, L., Klygin, S., Krupko, S., Meshkov, I. N., Rodin, A., Sereda, Y., Seleznev, I., Sidorchuk, S., Syresin, E., Stepantsov, S., Ter-Akopian, G., Teterev, Y., Vorontsov, A. N., Kamerdzhiev, S. P., Litvinova, E. V., Karataglidis, S., Alvarezrodriguez, R., Borge, M. J. G., Fernandezramirez, C., Garrido, E., Sarriguren, P., Vignote, J. R., Fraileprieto, L. M., Lopezherraiz, J., Moyadeguera, E., Udias-Moinelo, J., Amarosoriano, J. E., Lallena Rojo, A. M., Caballero, J. A., Johansson, H. T., Jonson, B., Nilsson, T., Nyman, G., Zhukov, M., Avdeichikov, V., Hencken, K., Jourdan, J., Krusche, B., Rauscher, T., Kiselev, D., Trautmann, D., Al-Khalili, J., Catford, W., Johnson, R., Stevenson, P., Barton, C., Jenkins, D., Lemmon, R., Chartier, M., Cullen, D., Heinz, A., Bertulani, C. A., Antonov, A. N., Gaidarov, M. K., Ivanov, M. V., Kadrev, D. N., Aïche, M., Barreau, G., Czajkowski, S., Jurado, B., Belier, G., Chatillon, A., Granier, T., Taieb, J., Doré, D., Letourneaux, A., Ridikas, D., Dupont, E., Berthoumieux, E., Panebianco, S., Reymund, F., Schmitt, C., Audouin, L., Khan, E., Tassan-Got, L., Aumann, T., Beller, P., Boretzky, K., Dolinskii, A., Egelhof, P., Emling, H., Franzke, B., Geissel, H., Kelic-Heil, A., Kester, O., Kurz, N., Litvinov, Y., Münzenberg, G., Nolden, F., Schmidt, K.-H., Simon, H., Steck, M., Weick, H., Enders, J., Pietralla, N., Richter, A., Schrieder, G., Zilges, A., Distler, M. O., Merkel, H., Müller, U., Junghans, A., Lenske, H., Fujiwara, M., Suda, T., Kato, S., Adachi, T., Hamieh, S., Harakeh, M. N., Kalantar-Nayestanaki, N., Wörtche, H., Berg, G. P. A., Koop, I. A., Logatchov, P. V., Otboev, A. V., Parkhomchuk, V. V., Shatilov, D. N., Shatunov, P. Y., Shatunov, Y. M., Shiyankov, S. V., Shvartz, D. I., Skrinsky, A. N., Chulkov, L. V., Danilin, B. V., Korsheninnikov, A. A., Kuzmin, E. A., Ogloblin, A. A., Volkov, V. A., Grishkin, Y., Lisin, V. P., Mushkarenkov, A. N., Nedorezov, V., Polonski, A. L., Rudnev, N. V., Turinge, A. A., Artukh, A., Ershov, S. N., Fomichev, A., Golovkov, M., Gorshkov, A. V., Grigorenko, L., Klygin, S., Krupko, S., Meshkov, I. N., Rodin, A., Sereda, Y., Seleznev, I., Sidorchuk, S., Syresin, E., Stepantsov, S., Ter-Akopian, G., Teterev, Y., Vorontsov, A. N., Kamerdzhiev, S. P., Litvinova, E. V., Karataglidis, S., Alvarezrodriguez, R., Borge, M. J. G., Fernandezramirez, C., Garrido, E., Sarriguren, P., Vignote, J. R., Fraileprieto, L. M., Lopezherraiz, J., Moyadeguera, E., Udias-Moinelo, J., Amarosoriano, J. E., Lallena Rojo, A. M., Caballero, J. A., Johansson, H. T., Jonson, B., Nilsson, T., Nyman, G., Zhukov, M., Avdeichikov, V., Hencken, K., Jourdan, J., Krusche, B., Rauscher, T., Kiselev, D., Trautmann, D., Al-Khalili, J., Catford, W., Johnson, R., Stevenson, P., Barton, C., Jenkins, D., Lemmon, R., Chartier, M., Cullen, D., Heinz, A., and Bertulani, C. A.

Abstract

The Electron-Ion Scattering experiment ELISe at the International Facility for Antiproton and Ion Research (FAIR) – a conceptual design study

Published
2011

8. Neutrons produits dans des cibles epaisses de Be et $^{238}$U par des deutons de 100 MeV/A et de C par des $^{36}$Ar de 95 MeV/A - Debit de dose resultant de l'activation de l'uranium

Author

Pauwels, N., Proust, J., Clapier, F., Gara, P., Mirea, M., Obert, J., Granier, T., Belier, G., Ethvignot, T., Liang, C F., Villari, A.C.C., Bajard, M., Leroy, R., Institut de Physique Nucléaire d'Orsay (IPNO), Université Paris-Sud - Paris 11 (UP11)-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Centre National de la Recherche Scientifique (CNRS), Grand Accélérateur National d'Ions Lourds (GANIL), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Centre National de la Recherche Scientifique (CNRS), GANIL, and Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)

Subjects
Health Physics and Radiation Effects, [PHYS.NEXP]Physics [physics]/Nuclear Experiment [nucl-ex]
Abstract

La production de faisceaux d'ions est un sujet qui intéressent de nombreux laboratoires.

Published
1998

9. Accurate measurement of $F_{2}^{\rm d}/F_{2}^{\rm p}$ and $R^{\rm d} - R^{\rm p}$

Author

Arneodo, M., Arvidson, A., Badełek, B., Ballintijn, M., Baum, G., Beaufays, J., Bird, I.G., Björkholm, P., Botje, M., Broggini, C., Brückner, W., Brüll, A., Burger, W.J., Ciborowski, J., van Dantzig, R., Dyring, A., Engelien, H., Ferrero, M.I., Fluri, L., Gaul, U., Granier, T., Grosse-Perdekamp, M., von Harrach, D., van der Heijden, M., Heusch, C., Ingram, Q., de Jong, M., Kabuβ, E.M., Kaiser, R., Ketel, T.J., Klein, F., Kullander, S., Landgraf, U., Lindqvist, T., Mallot, G.K., Mariotti, C., van Middelkoop, G., Milsztajn, A., Mizuno, Y., Most, A., Mücklich, A., Nassalski, J., Nowotny, D., Oberski, J., Paić, A., Peroni, C., Povh, B., Prytz, K., Rieger, R., Rith, K., Röhrich, K., Rondio, E., Ropelewski, L., Sandacz, A., Sanders, D., Scholz, C., Seitz, R., Sever, F., Shibata, T.-A., Siebler, M., Simon, A., Staiano, A., Szleper, M., Tłaczała, W., Tzamouranis, Y., Virchaux, M., Vuilleumier, J.L., Walcher, T., Windmolders, R., Witzmann, A., Zaremba, K., and Zetsche, F.

Subjects
Particle Physics - Experiment
Abstract

Results are presented for $F_{2}^{\rm d}/F_{2}^{\rm p}$ and $R^{\rm d} - R^{\rm p}$ from simultaneous measurements of deep inelastic muon scattering on hydrogen and deuterium targets, at 90, 120, 200 and 280 GeV. The difference $R^{\rm d} - R^{\rm p}$, determined in the range $0.0020.1$ the ratio decreases with $Q^{2}$. Results are presented for F 2 d / F 2 p and R d − R p from simultaneous measurements of deep inelastic muon scattering on hydrogen and deuterium targets, at 90, 120, 200 and 280 GeV. The difference R d − R p , determined in the range 0.002 < x < 0.4 at an average Q 2 of 5 GeV 2 , is compatible with zero. The x and Q 2 dependence of F 2 d / F 2 p was measured in the kinematic range 0.001 < x < 0.8 and 0.1 < Q 2 < 145 GeV 2 with small statistical and systematic errors. For x > 0.1 the ratio decreases with Q 2 . Results are presented for F2d/F2p and Rd-Rp from simultaneous measurements of deep inelastic muon scattering on hydrogen and deuterium targets, at 90, 120, 200 and 280 GeV. The difference Rd-Rp, determined in the range 0.0020.1 the ratio decreases with Q^2.

Published
1996

10. A re-evaluation of the nuclear structure function ratios for D, He, Li C and Ca

Author

Amaudruz, P., Arneodo, M., Arvidson, A., Badelek, B., Ballintijn, M., Baum, G., Beaufays, J., Bird, I.G., Björkholm, P., Botje, M., Broggini, C., Brückner, W., Brüll, A., Burger, W.J., Ciborowski, J., van Dantzig, R., Döbbeling, H., Domingo, J., Drinkard, J., Dyring, A., Engelien, H., Ferrero, M.I., Fluri, L., Gaul, U., Grafstrom, P., Granier, T., von Harrach, D., van der Heijden, M., Heusch, C., Ingram, Q., Janson-Prytz, K., de Jong, M., Kabuβ, E.M., Kaiser, R., Ketel, T.J., Klein, F., Korzen, B., Krüner, U., Kullander, S., Landgraf, U., Lettenström, F., Lindqvist, T., Mallot, G.K., Mariotti, C., van Middelkoop, G., Milsztajn, A., Mizuno, Y., Most, A., Mücklich, A., Nassalski, J., Nowotny, D., Pavel, N., Oberski, J., Paić, A., Peroni, C., Peschel, H., Povh, B., Rieger, R., Rith, K., Röhrich, K., Rondio, E., Ropelewski, L., Sandacz, A., Sanders, D., Scholz, C., Schumacher, R., Seitz, R., Sennhauser, U., Sever, F., Shibata, T.-A., Siebler, M., Simon, A., Staiano, A., Szleper, M., Taylor, G., Treichel, M., Tzamouranis, Y., Virchaux, M., Vuilleumier, J.L., Walcher, T., Windmolders, R., Witzmann, A., and Zetsche, F.

Subjects
Particle Physics - Experiment
Abstract

We present a re-evaluation of the structure function ratios F2(He)/F2(D), F2(C)/F2(D) and F2(Ca)/F2(D) measured in deep inelastic muon-nucleus scattering at an incident muon momentum of 200 GeV. We also present the ratios F2(C)/F2(Li), F2(Ca)/F2(Li) and F2(Ca)/F2(C) measured at 90 GeV. The results are based on data already published by NMC; the main difference in the analysis is a correction for the masses of the deuterium targets and an improvement in the radiative corrections. The kinematic range covered is 0.0035 < x < 0.65, 0.5 < Q^2

Published
1995

13. Exclusive $\varrho^{0}$ and $\phi$ muoproduction at large $Q^{2}$

Author

Arneodo, M, Arvidson, A, Badelek, B, Ballintijn, M K, Baum, G, Beaufays, J, Bird, I G, Björkholm, P, Botje, M, Broggini, C, Brückner, W, Brüll, A, Burger, W J, Ciborowski, J, Van Dantzig, R, Dyring, A, Engelien, H, Ferrero, M I, Fluri, L, Gaul, U, Granier, T, Von Harrach, D, Van der Heijden, M, Heusch, C A, Ingram, Q, Janson-Prytz, K, De Jong, M, Kabuss, E M, Kaiser, R, Ketel, T, Klein, F, Kullander, Sven, Kurek, K, Landgraf, U, Lindqvist, T, Mallot, G K, Mariotti, C, Van Middelkoop, G, Mizuno, Y, Most, A, Mücklich, A, Nassalski, J P, Nowotny, D, Oberski, J, Paic, A, Peroni, C, Povh, B, Rieger, R, Rith, K, Röhrich, K, Rondio, Ewa, Ropelewski, Leszek, Sandacz, A, Sanders, D, Scholz, C, Seitz, R, Sever, F, Shibata, T A, Siebler, M, Simon, A, Staiano, A, Szleper, M, Tzamouranis, Yu, Vuilleumier, J L, Walcher, T, Windmolders, R, Witzmann, A, and Zetsche, F

Subjects
Particle Physics - Experiment
Published
1994

14. Reevaluation of the Gottfried Sum

Author

Arneodo, M., Arvidson, A., Bruckner, W., Brull, A., Burger, W. J., Ciborowski, J., van Dantzig, R., Dyring, A., Engelien, H., Ferrero, M. I., Fluri, L., Gaul, U., Badelek, B., Granier, T., von Harrach, D., van der Heijden, M., Heusch, C., Ingram, C. H. Quentin, Janson-Prytz, K., de Jong, M., Kabuss, E. M., Kaiser, R., Ketel, T. J., Ballintijn, M., Klein, F., Kullander, S., Landgraf, U., Lindqvist, T., Mallot, G. K., Mariotti, C., van Middelkoop, G., Milsztajn, A., Mizuno, Y., Nassalski, J., Baum, Guenter, Oberski, J., Nowotny, D., Paic, A., Peroni, C., Povh, B., Rieger, R., Rith, K., Rohrich, K., Rondio, E., Ropelewski, L., Beaufays, J., Sandacz, A., Sanders, D., Scholz, C., Schumacher, R., Seitz, R., Sever, F., Shibata, T. A., Siebler, M., Simon, A., Staiano, A., Bird, I. G., Szleper, M., Tzamouranis, Y., Virchaux, M., Vuilleumier, J. L., Walcher, T., Windmolders, R., Witzmann, A., Zetsche, F., NMC Collaboration, Bjorkholm, P., Botje, M., and Broggini, C.

Subjects
Particle physics, difference [structure function], ratio [structure function], structure function [n], n: structure function, Gottfried [sum rule], RATIO F2(N)/F2(P), structure function [p], small-x [structure function], Combinatorics, numerical calculations: interpretation of experiments, INELASTIC MUON SCATTERING, interpretation of experiments [numerical calculations], radiative correction, ddc:530, structure function: difference, p: structure function, sum rule: Gottfried, Physics, structure function [deuteron], Structure function, deuteron: structure function, structure function: ratio, model: quark parton, x-dependence [structure function], structure function: x-dependence, structure function: small-x, quark parton [model], ELECTROMAGNETIC CORRECTIONS, Particle Physics - Experiment
Abstract

Physical review / D 50(1), R1 - R3 (1994). doi:10.1103/PhysRevD.50.R1, We present a new determination of the nonsinglet structure function ${\mathit{F}}_{2}^{\mathit{p}}$ - ${\mathit{F}}_{2}^{\mathit{n}}$ at ${\mathit{Q}}^{2}$=4 ${\mathrm{GeV}}^{2}$ using recently measured values of ${\mathit{F}}_{2}^{\mathit{d}}$ and ${\mathit{F}}_{2}^{\mathit{n}}$/${\mathit{F}}_{2}^{\mathit{p}}$. A new evaluation of the Gottfried sum is given, which remains below the simple quark-parton model value of 1/3., Published by Inst., Woodbury, NY

Published
1994

16. A re-evaluation of $F_{2}^{n}/F_{2}^{p}$ and $F_{2}^{p}-F_{2}^{n}$

Author

Arneodo, M, Arvidson, A, Badelek, B, Ballintijn, M K, Baum, G, Beaufays, J, Bird, I G, Björkholm, P, Botje, M, Broggini, C, Brückner, W, Brüll, A, Burger, W J, Ciborowski, J, Van Dantzig, R, Dyring, A, Engelien, H, Ferrero, M I, Fluri, L, Gaul, U, Granier, T, Von Harrach, D, Van der Heijden, M, Heusch, C A, Ingram, Q, Janson-Prytz, K, De Jong, M, Kabuss, E M, Kaiser, R, Ketel, T, Klein, F, Kullander, Sven, Landgraf, U, Lindqvist, T, Mallot, G K, Mariotti, C, Van Middelkoop, G, Milshtein, A I, Mizuno, Y, Nassalski, J P, Oberski, J, Nowotny, D, Paic, A, Peroni, C, Povh, B, Rieger, R, Rith, K, Röhrich, K, Rondio, Ewa, Ropelewski, Leszek, Sandacz, A, Sanders, D, Scholz, C, Schumacher, R, Seitz, R, Sever, F, Shibata, T A, Siebler, M, Simon, A, Staiano, A, Szleper, M, Tzamouranis, Yu, Virchaux, M, Vuilleumier, J L, Walcher, T, Windmolders, R, Witzmann, A, and Zetsche, F

Subjects
Particle Physics - Experiment
Published
1993

18. Evidence of new cadmium binding sites in recombinant horse L-chain ferritin by anomalous Fourier difference map calculation

Author

UCL, Granier, T, Comberton, G, Gallois, B, d'Estaintot, BL, Dautant, A, Crichton, Robert, Precigoux, G, UCL, Granier, T, Comberton, G, Gallois, B, d'Estaintot, BL, Dautant, A, Crichton, Robert, and Precigoux, G

Abstract

We refined the structure of the tetragonal form of recombinant horse L-chain apoferritin to 2.0 Angstrom and we compared it with that of the cubic form previously refined to the same resolution, The major differences between the two structures concern the cadmium ions bound to the residues E130 at the threefold axes of the molecule, Taking advantage of the significant anomalous signal (f" = 3.6 e(-)) of cadmium at 1.375 Angstrom, the wavelength used here, we performed anomalous Fourier difference maps with the refined model phases. These maps reveal the positions of anomalous scatterers at different locations in the structure, Among these, some are found near residues that were known previously to bind metal ions, C48, E57, C126, D127, E130, and H132. But new cadmium binding sites are evidenced near residues E53, E56, E57, E60, and H114, which were suggested to be involved in the iron loading process. The quality of the anomalous Fourier difference map increases significantly with noncrystallographic symmetry map averaging. Such maps reveal density peaks that fit the positions of Met and Cys sulfur atoms, which are weak anomalous scatterers (f" = 0.44 e(-)). (C) 1998 Wiley-Liss, Inc.

Published
1998

19. Measurement of the proton and deuteron structure functions, F-2(p) and F-2(d), and of the ratio sigma(L)/sigma(T)

Author

Arneodo, M, Arvidson, A, Badelek, B, Ballintijn, M, Baum, G, Beaufays, J, Bird, IG, Bjorkholm, P, Botje, M, Broggini, C, Bruckner, W, Brull, A, Burger, WJ, Ciborowski, J, vanDantzig, R, Dyring, A, Engelien, H, Ferrero, MI, Fluri, L, Gaul, U, Granier, T, GrossePerdekamp, M, von, Arneodo, M, Arvidson, A, Badelek, B, Ballintijn, M, Baum, G, Beaufays, J, Bird, IG, Bjorkholm, P, Botje, M, Broggini, C, Bruckner, W, Brull, A, Burger, WJ, Ciborowski, J, vanDantzig, R, Dyring, A, Engelien, H, Ferrero, MI, Fluri, L, Gaul, U, Granier, T, GrossePerdekamp, M, and von

Abstract

The muon-proton and muon-deuteron inclusive deep inelastic scattering cross sections were measured in the kinematic range 0.002 < x < 0.60 and 0.5 < Q(2) < 75 GeV2 at incident muon energies of 90, 120, 200 and 280 GeV. These results are based on the full, Addresses: Arneodo M, UNIV TURIN, I-10124 TURIN, ITALY. UNIV BIELEFELD, D-4800 BIELEFELD, GERMANY. UNIV FREIBURG, FREIBURG, GERMANY. MAX PLANCK INST KERNPHYS, D-69117 HEIDELBERG, GERMANY. UNIV HEIDELBERG, D-6900 HEIDELBERG, GERMANY. UNIV MAINZ, D-6500 MAI

Published
1997

20. Accurate measurement of F-2(d)/F-2(p) and R(d)-R(p)

Author

Arneodo, M, Arvidson, A, Badelek, B, Ballintijn, M, Baum, G, Beaufays, J, Bird, IG, Bjorkholm, P, Botje, M, Broggini, C, Bruckner, W, Brull, A, Burger, WJ, Ciborowski, J, vanDantzig, R, Dyring, A, Engelien, H, Ferrero, MI, Fluri, L, Gaul, U, Granier, T, GrossePerdekamp, M, von, Arneodo, M, Arvidson, A, Badelek, B, Ballintijn, M, Baum, G, Beaufays, J, Bird, IG, Bjorkholm, P, Botje, M, Broggini, C, Bruckner, W, Brull, A, Burger, WJ, Ciborowski, J, vanDantzig, R, Dyring, A, Engelien, H, Ferrero, MI, Fluri, L, Gaul, U, Granier, T, GrossePerdekamp, M, and von

Abstract

Results are presented for F-2(d)/F-2(p) and R(d) - R(p) from simultaneous measurements of deep inelastic muon scattering on hydrogen and deuterium targets, at 90, 120, 200 and 280 GeV. The difference R(d) - R(p), determined in the range 0.002 < x < 0.4 at, Addresses: Arneodo M, UNIV TURIN, I-10124 TURIN, ITALY. IST NAZL FIS NUCL, I-10125 TURIN, ITALY. UNIV BIELEFELD, D-4800 BIELEFELD, GERMANY. UNIV FREIBURG, D-7800 FREIBURG, GERMANY. MAX PLANCK INST KERNPHYS, D-69117 HEIDELBERG, GERMANY. UNIV HEIDELBERG, D

Published
1997

21. X-ray structure of recombinant horse L-chain apoferritin at 2.0 angstrom resolution: Implications for stability and function

Author

UCL, Gallois, B, dEstaintot, BL, Michaux, MA, Dautant, A, Granier, T, Precigoux, G, Soruco, JA, Roland, Francine, ChavasAlba, O, Herbas, A, Crichton, Robert, UCL, Gallois, B, dEstaintot, BL, Michaux, MA, Dautant, A, Granier, T, Precigoux, G, Soruco, JA, Roland, Francine, ChavasAlba, O, Herbas, A, and Crichton, Robert

Abstract

The X-ray structure of recombinant horse L-chain (rL) apoferritin, solved at 2.0 Angstrom resolution with a final R factor of 17.99 %. gives evidence that the residue at position 93 in the sequence is a proline and not a leucine. as found in earlier sequencing studies, The structure is isomorphous with other apoferritin structures, and we thus draw particular attention to those structural features which can be related to the stability and function of the protein. Analysis of hydrogen bonding and salt bridge interactions shows a that dimers and tetramers are the most stable molecular entities within the protein shell: a result confirming earlier biophysical experiments, The stability of horse rL apoferritin to both dissociation into subunits at acidic pH values and to complete unfolding in guanidine chloride solutions is compared with that of other apoferritins. This emphasizes the role played by the salt bridge in the stability of this protein family, The horse rL apoferritin is significantly more resistant to denaturation than horse spleen ferritin, which in turn is more resistant than any human rH apoferritins, even those for which a salt bridge is restored. Finally this structure determination not only establishes that a preformed pocket exists in L-chain apoferritin, at a site known to be able to bind porphyrin. but also underlines the particular function of a cluster of glutamic acids (E53, E56, E57 and E60) located at the entrance of this porphyrin-binding pocket.

Published
1997

23. The Q(2) dependence of the structure function ratio F-2(Sn)/F-2(C) and the difference R(Sn)-R(C) in deep inelastic muon scattering

Author

Arneodo, M, Arvidson, A, Badelek, B, Ballintijn, M, Baum, G, Beaufays, J, Bird, IG, Bjorkholm, P, Botje, M, Broggini, C, Bruckner, W, Brull, A, Burger, WJ, Ciborowski, J, vanDantzig, R, Dobbeling, H, Dyring, A, Engelien, H, Ferrero, MI, Fluri, L, Gaul, U, Granier, T, GrossePer, Arneodo, M, Arvidson, A, Badelek, B, Ballintijn, M, Baum, G, Beaufays, J, Bird, IG, Bjorkholm, P, Botje, M, Broggini, C, Bruckner, W, Brull, A, Burger, WJ, Ciborowski, J, vanDantzig, R, Dobbeling, H, Dyring, A, Engelien, H, Ferrero, MI, Fluri, L, Gaul, U, Granier, T, and GrossePer

Abstract

The Q(2) dependence of the structure function ratio F-2(Sn)/F-2(C) for 0.01 < x < 0.75 and 1 < Q(2) < 140 GeV2 is reported. For x < 0.1 the size of shadowing decreases linearly with In Q(2) and the maximum rate is about 0.04 at x = 0.01. The rate decrease, Addresses: Arneodo M, UNIV TURIN, TURIN, ITALY. UNIV BIELEFELD, D-4800 BIELEFELD, GERMANY. UNIV FREIBURG, FREIBURG, GERMANY. MAX PLANCK INST KERNPHYS, D-69117 HEIDELBERG, GERMANY. UNIV HEIDELBERG, HEIDELBERG, GERMANY. UNIV MAINZ, D-6500 MAINZ, GERMANY. UN

Published
1996

24. The A dependence of the nuclear structure function ratios

Author

Arneodo, M, Arvidson, A, Badelek, B, Ballintijn, M, Baum, G, Beaufays, J, Bird, IG, Bjorkholm, P, Botje, M, Broggini, C, Bruckner, W, Brull, A, Burger, WJ, Ciborowski, J, vanDantzig, R, Dyring, A, Engelien, H, Ferrero, MI, Fluri, L, Gaul, U, Granier, T, Grosseperdekamp, M, von, Arneodo, M, Arvidson, A, Badelek, B, Ballintijn, M, Baum, G, Beaufays, J, Bird, IG, Bjorkholm, P, Botje, M, Broggini, C, Bruckner, W, Brull, A, Burger, WJ, Ciborowski, J, vanDantzig, R, Dyring, A, Engelien, H, Ferrero, MI, Fluri, L, Gaul, U, Granier, T, Grosseperdekamp, M, and von

Abstract

Results are presented for six nuclei from Be to Pb on the structure function ratios F-2(A)/F-2(C)(X) and their A dependence in deep inelastic muon scattering at 200 GeV incident: muon energy. The data cover the kinematic range 0.01 < x < 0.8 with Q(2) ran, Addresses: Arneodo M, UNIV TURIN, TURIN, ITALY. UNIV BIELEFELD, D-4800 BIELEFELD, GERMANY. UNIV FREIBURG, FREIBURG, GERMANY. MAX PLANCK INST KERNPHYS, D-69117 HEIDELBERG, GERMANY. UNIV HEIDELBERG, HEIDELBERG, GERMANY. UNIV MAINZ, D-6500 MAINZ, GERMANY. UN

Published
1996

25. MEASUREMENT OF THE PROTON AND THE DEUTERON STRUCTURE FUNCTIONS, F-2(P) AND F-2(D)

Author

ARNEODO, M, ARVIDSON, A, BADELEK, B, BALLINTIJN, M, BAUM, G, BEAUFAYS, J, BIRD, IG, BJORKHOLM, P, BOTJE, M, BROGGINI, C, BRUCKNER, W, BRULL, A, BURGER, WJ, CIBOROWSKI, J, VANDANTZIG, R, DYRING, A, ENGELIEN, H, FERRERO, MI, FLURI, L, GAUL, U, GRANIER, T, GROSSEPERDEKAMP, M, VON, ARNEODO, M, ARVIDSON, A, BADELEK, B, BALLINTIJN, M, BAUM, G, BEAUFAYS, J, BIRD, IG, BJORKHOLM, P, BOTJE, M, BROGGINI, C, BRUCKNER, W, BRULL, A, BURGER, WJ, CIBOROWSKI, J, VANDANTZIG, R, DYRING, A, ENGELIEN, H, FERRERO, MI, FLURI, L, GAUL, U, GRANIER, T, GROSSEPERDEKAMP, M, and VON

Published
1995

26. THE STRUCTURE-FUNCTION RATIOS F-2(LI)/F-2(D) AND F-2(C)/F-2(D) AT SMALL-X

Author

ARNEODO, M, ARVIDSON, A, BADELEK, B, BALLINTIJN, M, BAUM, G, BEAUFAYS, J, BIRD, IG, BJORKHOLM, P, BOTJE, M, BROGGINI, C, BRUCKNER, W, BRULL, A, BURGER, WJ, CIBOROWSKI, J, VANDANTZIG, R, DYRING, A, ENGELIEN, H, FERRERO, MI, FLURI, L, GAUL, U, GRANIER, T, GROSSEPERDEKAMP, M, VON, ARNEODO, M, ARVIDSON, A, BADELEK, B, BALLINTIJN, M, BAUM, G, BEAUFAYS, J, BIRD, IG, BJORKHOLM, P, BOTJE, M, BROGGINI, C, BRUCKNER, W, BRULL, A, BURGER, WJ, CIBOROWSKI, J, VANDANTZIG, R, DYRING, A, ENGELIEN, H, FERRERO, MI, FLURI, L, GAUL, U, GRANIER, T, GROSSEPERDEKAMP, M, and VON

Abstract

We present the structure function ratios F-2(Li)/F-2(D) and F-2(C)/F-2(D) measured in deep inelastic muon-nucleus scattering at a nominal incident muon energy of 200 GeV. The kinematic range 10(-4) < x < 0.7 and 0.01 < Q(2) < 70 GeV2 is covered. For value, Addresses: UNIV BIELEFELD, W-4800 BIELEFELD, GERMANY. UNIV FREIBURG, FREIBURG, GERMANY. MAX PLANCK INST KERNPHYS, HEIDELBERG, GERMANY. UNIV HEIDELBERG, HEIDELBERG, GERMANY. UNIV MAINZ, W-6500 MAINZ, GERMANY. UNIV MONS, B-7000 MONS, BELGIUM. UNIV NEUCHATEL

Published
1995

27. Neutrons produits dans des cibles épaisses de Be et 238U irradiées par des deutons de 100 MeV/u et dans une cible épaisse de C irradiée par des 36Ar de 95 MeV/u. Longueurs d'atténuation dans du béton et débit d'équivalent de dose résultant de lactivation de l'uranium

Author

Pauwels, N., primary, Proust, J., additional, Bajard, M., additional, Bélier, G., additional, Clapier, F., additional, Ethvignot, T., additional, Gara, P., additional, Granier, T., additional, Leroy, R., additional, Liang, C. F., additional, Mirea, M., additional, Obert, J., additional, and Villari, A. C. C., additional

Published
1999
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29. Spectrum of prompt fission neutrons from U( n, F).

Author

Maslov, V., Tetereva, N., Pronyaev, V., Kagalenko, A., Zolotarev, K., Capote, R., Granier, T., Morillon, B., Hambsch, F.-J., and Sublet, J.-C.

Subjects
THERMAL neutron spectra, NUCLEAR fission, NUCLEAR reactions, NUCLEAR energy, NUCLEAR engineering, PHYSICAL measurements
Abstract

new matrix of the spectra of prompt fission neutrons for the reaction U( n, F) has been obtained. The evaluated spectrum of prompt fission neutrons reproduces the measured data for incident neutrons with energy from thermal to 14.7 MeV. A solution is proposed for the problem of inconsistency of the integral testing of the systems with a thermal spectrum and differential measurements of the spectra of prompt fission neutrons. The matrix obtained for the spectra of prompt neutrons for U( n, F) eliminates the considerable discrepancy between the differential and integral experiments. The description of the integral experiments for compositions with a fast neutron spectrum revealed the compensation effect in the multiplication factor K, due to the difference in the shapes of the spectra of prompt fission neutrons, the present work and known libraries. The description of systems with a thermal neutron spectrum shows that the positive shift of the computed K is explained by the influence of the low-energy neutrons. [ABSTRACT FROM AUTHOR]

Published
2010
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33. Mutant ferritin L-chains that cause neurodegeneration act in a dominant negative manner to reduce ferritin iron incorporation

Author

Bernard Gallois, Angela Cattaneo, Anna Cozzi, Paolo Santambrogio, Dario Finazzi, Béatrice Langlois d'Estaintot, Sonia Levi, Paolo Arosio, Sara Luscieti, Maura Poli, Thierry Granier, Luscieti, S, Santambrogio, P, LANGLOIS D'ESTAINTOT, B, Granier, T, Cozzi, A, Poli, M, Gallois, B, Finazzi, D, Cattaneo, A, Levi, SONIA MARIA ROSA, and Arosio, P.

Subjects
Models, Molecular, Spectrometry, Mass, Electrospray Ionization, Protein Conformation, Iron, Molecular Sequence Data, Static Electricity, Mutant, Neuroferritinopathy, In Vitro Techniques, Crystallography, X-Ray, medicine.disease_cause, Biochemistry, Protein structure, medicine, Humans, Amino Acid Sequence, Molecular Biology, Peptide sequence, Genes, Dominant, Sequence Deletion, Mutation, biology, Protein Stability, Chemistry, Neurodegeneration, Molecular Bases of Disease, Cell Biology, medicine.disease, Recombinant Proteins, Ferritin light chain, Ferritin, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Apoferritins, Nerve Degeneration, biology.protein, Hydrophobic and Hydrophilic Interactions
Abstract

Nucleotide insertions that modify the C terminus of ferritin light chain (FTL) cause neurodegenerative movement disorders named neuroferritinopathies, which are inherited with dominant transmission. The disorders are characterized by abnormal brain iron accumulation. Here we describe the biochemical and crystallographic characterization of pathogenic FTL mutant p.Phe167SerfsX26 showing that it is a functional ferritin with an altered conformation of the C terminus. Moreover we analyze functional and stability properties of ferritin heteropolymers made of 20–23 H-chains and 1–4 L-chains with representative pathogenic mutations or the last 10–28 residues truncated. All the heteropolymers containing the pathogenic or truncated mutants had a strongly reduced capacity to incorporate iron, both when expressed in Escherichia coli, and in vitro when iron was supplied as Fe(III) in the presence of ascorbate. The mutations also reduced the physical stability of the heteropolymers. The data indicate that even a few mutated L-chains are sufficient to alter the permeability of 1–2 of the 6 hydrophobic channels and modify ferritin capacity to incorporate iron. The dominant-negative action of the mutations explains the dominant transmission of the disorder. The data support the hypothesis that hereditary ferritinopathies are due to alterations of ferritin functionality and provide new input on the mechanism of the function of isoferritins.

Published
2010

34. Crystal structure and biochemical properties of the human mitochondrial ferritin and its mutant Ser144Ala

Author

Thierry Granier, Jean Marc Chevalier, Gilles Precigoux, Paolo Santambrogio, Bernard Gallois, Béatrice Langlois d'Estaintot, Paolo Arosio, Sonia Levi, LANGLOIS D'ESTAINTOT, B, Santambrogio, P, Granier, T, Gallois, B, Chevalier, Jm, Precigoux, G, Levi, SONIA MARIA ROSA, and Arosio, P.

Subjects
Models, Molecular, Protein Denaturation, Protein Conformation, Mutant, Molecular Sequence Data, Mitochondrion, Ferroxidase activity, Crystallography, X-Ray, Structural Biology, Serine, Humans, Amino Acid Sequence, Protein precursor, Molecular Biology, Manganese, Binding Sites, biology, Sequence Homology, Amino Acid, Chemistry, MITOCHONDRIAL FERRITIN, Mitochondria, Ferritin, A-site, Zinc, Biochemistry, Mutagenesis, Ferritins, biology.protein, Ceruloplasmin
Abstract

Mitochondrial ferritin is a recently identified protein precursor encoded by an intronless gene. It is specifically taken up by the mitochondria and processed to a mature protein that assembles into functional ferritin shells. The full mature recombinant protein and its S144A mutant were produced to study structural and functional properties. They yielded high quality crystals from Mg(II) solutions which diffracted up to 1.38 Angstrom resolution. The 3D structures of the two proteins resulted very similar to that of human H-ferritin, to which they have high level of sequence identity (approximately 80%). Metal-binding sites were identified in the native crystals and in those soaked in Mn(II) and Zn(II) solutions. The ferroxidase center binds binuclear iron at the sites A and B, and the structures showed that the A site was always fully occupied by Mg(II), Mn(II) or Zn(II), while the occupancy of the B site was variable. In addition, distinct Mg(II) and Zn(II)-binding sites were found in the 3-fold axes to block the hydrophilic channels. Other metal-binding sites, never observed before in H-ferritin, were found on the cavity surface near the ferroxidase center and near the 4-fold axes. Mitochondrial ferritin showed biochemical properties remarkably similar to those of human H-ferritin, except for the difficulty in renaturing to yield ferritin shells and for a reduced ( approximately 41%) rate in ferroxidase activity. This was partially rescued by the substitution of the bulkier Ser144 with Ala, which occurs in H-ferritin. The residue is exposed on a channel that connects the ferroxidase center with the cavity. The finding that the mutation increased both catalytic activity and the occupancy of the B site demonstrated that the channel is functionally important. In conclusion, the present data define the structure of human mitochondrial ferritin and provide new data on the iron pathways within the H-type ferritin shell.

Published
2004

36. Aromatic foldamers as scaffolds for metal second coordination sphere design.

Author

Meunier A, Singleton ML, Kauffmann B, Granier T, Lautrette G, Ferrand Y, and Huc I

Abstract

As metalloproteins exemplify, the chemical and physical properties of metal centers depend not only on their first but also on their second coordination sphere. Installing arrays of functional groups around the first coordination sphere of synthetic metal complexes is thus highly desirable, but it remains a challenging objective. Here we introduce a novel approach to produce tailored second coordination spheres. We used bioinspired artificial architectures based on aromatic oligoamide foldamers to construct a rigid, modular and well-defined environment around a metal complex. Specifically, aza-aromatic monomers having a tethered [2Fe-2S] cluster have been synthesized and incorporated in conical helical foldamer sequences. Exploiting the modularity and predictability of aromatic oligoamide structures allowed for the straightforward design of a conical architecture able to sequester the metal complex in a confined environment. Even though no direct metal complex-foldamer interactions were purposely designed in this first generation model, crystallography, NMR and IR spectroscopy concurred to show that the aromatic oligoamide backbone alters the structure and fluxional processes of the metal cluster., Competing Interests: There are no conflicts to declare., (This journal is © The Royal Society of Chemistry.)

Published
2020
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37. A single amino acid change within the R2 domain of the VvMYB5b transcription factor modulates affinity for protein partners and target promoters selectivity.

Author

Hichri I, Deluc L, Barrieu F, Bogs J, Mahjoub A, Regad F, Gallois B, Granier T, Trossat-Magnin C, Gomès E, and Lauvergeat V

Subjects
Amino Acid Sequence, Amino Acid Substitution, Basic Helix-Loop-Helix Transcription Factors metabolism, Flavonoids biosynthesis, Flavonoids genetics, Gene Expression Regulation, Plant, Genes, myb, Models, Molecular, Molecular Sequence Data, Phenotype, Plant Proteins genetics, Plants, Genetically Modified genetics, Plants, Genetically Modified metabolism, Protein Structure, Tertiary, RNA, Plant genetics, Nicotiana genetics, Nicotiana metabolism, Transcription Factors genetics, Two-Hybrid System Techniques, Vitis metabolism, Plant Proteins metabolism, Transcription Factors metabolism, Vitis genetics
Abstract

Background: Flavonoid pathway is spatially and temporally controlled during plant development and the transcriptional regulation of the structural genes is mostly orchestrated by a ternary protein complex that involves three classes of transcription factors (R2-R3-MYB, bHLH and WDR). In grapevine (Vitis vinifera L.), several MYB transcription factors have been identified but the interactions with their putative bHLH partners to regulate specific branches of the flavonoid pathway are still poorly understood., Results: In this work, we describe the effects of a single amino acid substitution (R69L) located in the R2 domain of VvMYB5b and predicted to affect the formation of a salt bridge within the protein. The activity of the mutated protein (name VvMYB5b(L), the native protein being referred as VvMYB5b(R)) was assessed in different in vivo systems: yeast, grape cell suspensions, and tobacco. In the first two systems, VvMYB5b(L) exhibited a modified trans-activation capability. Moreover, using yeast two-hybrid assay, we demonstrated that modification of VvMYB5b transcriptional properties impaired its ability to correctly interact with VvMYC1, a grape bHLH protein. These results were further substantiated by overexpression of VvMYB5b(R) and VvMYB5b(L) genes in tobacco. Flowers from 35S::VvMYB5b(L) transgenic plants showed a distinct phenotype in comparison with 35S::VvMYB5b(R) and the control plants. Finally, significant differences in transcript abundance of flavonoid metabolism genes were observed along with variations in pigments accumulation., Conclusions: Taken together, our findings indicate that VvMYB5b(L) is still able to bind DNA but the structural consequences linked to the mutation affect the capacity of the protein to activate the transcription of some flavonoid genes by modifying the interaction with its co-partner(s). In addition, this study underlines the importance of an internal salt bridge for protein conformation and thus for the establishment of protein-protein interactions between MYB and bHLH transcription factors. Mechanisms underlying these interactions are discussed and a model is proposed to explain the transcriptional activity of VvMYB5(L) observed in the tobacco model.

Published
2011
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38. Mutant ferritin L-chains that cause neurodegeneration act in a dominant-negative manner to reduce ferritin iron incorporation.

Author

Luscieti S, Santambrogio P, Langlois d'Estaintot B, Granier T, Cozzi A, Poli M, Gallois B, Finazzi D, Cattaneo A, Levi S, and Arosio P

Subjects
Amino Acid Sequence, Apoferritins chemistry, Crystallography, X-Ray, Genes, Dominant, Humans, Hydrophobic and Hydrophilic Interactions, In Vitro Techniques, Models, Molecular, Molecular Sequence Data, Nerve Degeneration etiology, Protein Conformation, Protein Stability, Recombinant Proteins chemistry, Recombinant Proteins genetics, Recombinant Proteins metabolism, Sequence Deletion, Spectrometry, Mass, Electrospray Ionization, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Static Electricity, Apoferritins genetics, Apoferritins metabolism, Iron metabolism, Mutation, Nerve Degeneration genetics, Nerve Degeneration metabolism
Abstract

Nucleotide insertions that modify the C terminus of ferritin light chain (FTL) cause neurodegenerative movement disorders named neuroferritinopathies, which are inherited with dominant transmission. The disorders are characterized by abnormal brain iron accumulation. Here we describe the biochemical and crystallographic characterization of pathogenic FTL mutant p.Phe167SerfsX26 showing that it is a functional ferritin with an altered conformation of the C terminus. Moreover we analyze functional and stability properties of ferritin heteropolymers made of 20-23 H-chains and 1-4 L-chains with representative pathogenic mutations or the last 10-28 residues truncated. All the heteropolymers containing the pathogenic or truncated mutants had a strongly reduced capacity to incorporate iron, both when expressed in Escherichia coli, and in vitro when iron was supplied as Fe(III) in the presence of ascorbate. The mutations also reduced the physical stability of the heteropolymers. The data indicate that even a few mutated L-chains are sufficient to alter the permeability of 1-2 of the 6 hydrophobic channels and modify ferritin capacity to incorporate iron. The dominant-negative action of the mutations explains the dominant transmission of the disorder. The data support the hypothesis that hereditary ferritinopathies are due to alterations of ferritin functionality and provide new input on the mechanism of the function of isoferritins.

Published
2010
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39. Membrane topography of the coupling ion binding site in Na+-translocating F1F0 ATP synthase.

Author

von Ballmoos C, Appoldt Y, Brunner J, Granier T, Vasella A, and Dimroth P

Subjects
Adenosine Triphosphatases isolation & purification, Binding Sites, Carbodiimides chemical synthesis, Cation Transport Proteins isolation & purification, Cell Membrane enzymology, Cell Membrane ultrastructure, Fusobacterium enzymology, Ions metabolism, Liposomes, Molecular Conformation, Phosphatidylcholines, Protein Subunits, Proton-Translocating ATPases isolation & purification, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Adenosine Triphosphatases chemistry, Cation Transport Proteins chemistry, Proton-Translocating ATPases chemistry, Sodium metabolism
Abstract

A carbodiimide with a photoactivatable diazirine substituent was synthesized and incubated with the Na(+)-translocating F(1)F(0) ATP synthase from both Propionigenium modestum and Ilyobacter tartaricus. This caused severe inhibition of ATP hydrolysis activity in the absence of Na(+) ions but not in its presence, indicating the specific reaction with the Na(+) binding c-Glu(65) residue. Photocross-linking was investigated with the substituted ATP synthase from both bacteria in reconstituted 1-palmitoyl-2-oleyl-sn-glycero-3-phosphocholine (POPC)-containing proteoliposomes. A subunit c/POPC conjugate was found in the illuminated samples but no a-c cross-links were observed, not even after ATP-induced rotation of the c-ring. Our substituted diazirine moiety on c-Glu(65) was therefore in close contact with phospholipid but does not contact subunit a. Na(+)in/(22)Na(+)out exchange activity of the ATP synthase was not affected by modifying the c-Glu(65) sites with the carbodiimide, but upon photoinduced cross-linking, this activity was abolished. Cross-linking the rotor to lipids apparently arrested rotational mobility required for moving Na(+) ions back and forth across the membrane. The site of cross-linking was analyzed by digestions of the substituted POPC using phospholipases C and A(2) and by mass spectroscopy. The substitutions were found exclusively at the fatty acid side chains, which indicates that c-Glu(65) is located within the core of the membrane.

Published
2002
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40. Spin crossover in a catenane supramolecular system.

Author

Real JA, Andrés E, Muñoz MC, Julve M, Granier T, Bousseksou A, and Varret F

Abstract

The compound [Fe(tvp)(2)(NCS)(2)] . CH(3)OH, where tvp is 1,2-di-(4-pyridyl)-ethylene, has been synthesized and characterized by x-ray single-crystal diffraction. It consists of two perpendicular, two-dimensional networks organized in parallel stacks of sheets made up of edge-shared [Fe(II)](4) rhombuses. The fully interlocked networks define large square channels in the [001] direction. Variable-temperature magnetic susceptibility measurements and Mössbauer studies reveal that this compound shows low-spin to high-spin crossover behavior in the temperature range from 100 to 250 kelvin. The combined structural and magnetic characterization of this kind of compound is fundamental for the interpretation of the mechanism leading to the spin crossover, which is important in the development of electronic devices such as molecular switches.

Published
1995
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