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Due to their high specific strength and temperature resistance, γ-titanium aluminides (γ-TiAl) have a growing importance for automotive and aerospace applications. However, conventional processing is very challenging due to the inherent brittleness of the material. Therefore, new manufacturing techniques and methods have to be established. Additive manufacturing techniques such as electron powder bed fusion (PBF-EB/M) are favored, since they enable near net shape manufacturing of highly complex geometries. The high preheating temperatures, which typically occur during PBF-EB/M, can significantly improve the processability of TiAl and facilitate the fabrication of complex parts. In this study, a previously optimized material condition of the β-solidifying TNM alloy TNM-B1 (Ti-43.5Al-4Nb-1Mo-0.1B) was manufactured by PBF-EB/M. The resulting microstructure, defect distribution and morphology, and mechanical properties were characterized by means of characterization methods, e.g., CT, SEM, light microscopy, hardness measurements, and tensile tests. A special focus was on the mechanical high-temperature behavior. The pronounced sensitivity of the material to defects and internal notches, e.g., due to lack of fusion defects (misconnections) which were found in the as-built condition, was identified as a main cause for premature failure below the yield point due to the low ductility. This failure was analyzed and potential improvements were identified.

Scaffolding proteins are essential for the assembly of most tailed, double-stranded DNA bacteriophages as well as herpesviruses. These proteins interact specifically with the coat proteins to efficiently assemble procapsids with the correct morphology. A helix-turn-helix (HTH) domain of bacteriophage P22 scaffolding protein is essential for coat binding, but the presence of additional coat protein binding sites has been predicted. An alanine substitution at scaffolding protein residue L245 causes a strong cold-sensitive phenotype. Bothin vivoandin vitroassembly with L245A scaffolding protein yields aberrant and petite particles at non-permissive temperatures. The L245A scaffolding protein is destabilized as determined by thermal melts monitored by circular dichroism. Through crosslinking studies, residue L245 interacts with the coat protein A-domain residue D198, which has been predicted previously to contain a scaffolding protein binding site. L245 also binds R101 in the coat protein P-domain as well as E18 in the N-arm. These results demonstrate the presence of secondary coat binding sites that may function in conjunction with the HTH domain to promote the assembly of procapsids with the correct curvature.ImportanceMany dsDNA viruses, including tailed bacteriophages and Herpesviruses, assemble precursor capsids, or procapsids, using an essential catalytic scaffolding protein. How scaffolding proteins induce proper assembly of their major capsid proteins remains unclear. The scaffolding protein of bacteriophage P22 has a C-terminal helix-turn-helix domain that interacts with the N-arm of the coat protein to activate it for assembly. Here, a second potential coat protein interaction site is identified in scaffolding protein at residue L245. Residue L245 may be involved in stabilizing a small helical domain based the effect of the substitution scaffolding protein stability and a predicted model of the scaffolding protein fold, thereby indicating additional complexity in the interaction between coat and scaffolding proteins.

Sf6 is a bacterial virus that infects the human pathogen Shigella flexneri. Here, we describe the cryo–electron microscopy structure of the Sf6 tail machine before DNA ejection, which we determined at a 2.7-angstrom resolution. We built de novo structures of all tail components and resolved four symmetry-mismatched interfaces. Unexpectedly, we found that the tail exists in two conformations, rotated by ~6° with respect to the capsid. The two tail conformers are identical in structure but differ solely in how the portal and head-to-tail adaptor carboxyl termini bond with the capsid at the fivefold vertex, similar to a diamond held over a five-pronged ring in two nonidentical states. Thus, in the mature Sf6 tail, the portal structure does not morph locally to accommodate the symmetry mismatch but exists in two energetic minima rotated by a discrete angle. We propose that the design principles of the Sf6 tail are conserved across P22-like Podoviridae.

Hydrodynamic radii (R (h)‐values) calculated from diffusion coefficients measured by pulse‐field‐gradient nuclear magnetic resonance are compared for folded and unfolded proteins. For native globular proteins, the R (h)‐values increase as a power of 0.35 with molecular size, close to the scaling factor of 0.33 predicted from polymer theory. Unfolded proteins were studied under four sets of conditions: in the absence of denaturants, in the presence of 6 M urea, in 95% dimethyl sulfoxide (DMSO), and in 40% hexafluoroisopropanol (HFIP). Scaling factors under all four unfolding conditions are similar (0.49–0.53) approaching the theoretical value of 0.60 for a fully unfolded random coil. Persistence lengths are also similar, except smaller in 95% DMSO, suggesting that the polypeptides are more disordered on a local scale with this solvent. Three of the proteins in our unfolded set have an asymmetric sequence‐distribution of charged residues. While these proteins behave normally in water and 6 M urea, they give atypically low R (h)‐values in 40% HFIP and 95% DMSO suggesting they are forming electrostatic hairpins, favored by their asymmetric sequence charge distribution and the low dielectric constants of DMSO and HFIP. While diffusion‐ordered NMR spectroscopy can separate small molecules, we show a number of factors combine to make protein‐sized molecules much more difficult to resolve in mixtures. Finally, we look at the temperature dependence of apparent diffusion coefficients. Small molecules show a linear temperature response, while large proteins show abnormally large apparent diffusion coefficients at high temperatures due to convection, suggesting diffusion reference standards are only useful near 25°C.

The oligomerization and incorporation of the bacteriophage P22 portal protein complex into procapsids (PCs) depends upon an interaction with scaffolding protein, but the region of the portal protein that interacts with scaffolding protein has not been defined. In herpes simplex virus 1 (HSV-1), conserved tryptophan residues located in the wing domain are required for portal-scaffolding protein interactions. In this study, tryptophan residues (W) present at positions 41, 44, 207 and 211 within the wing domain of the bacteriophage P22 portal protein were mutated to both conserved and non-conserved amino acids. Substitutions at each of these positions were shown to impair portal function in vivo, resulting in a lethal phenotype by complementation. The alanine substitutions caused the most severe defects and were thus further characterized. An analysis of infected cell lysates for the W to A mutants revealed that all the portal protein variants except W211A, which has a temperature-sensitive incorporation defect, were successfully recruited into procapsids. By charge detection mass spectrometry, all W to A mutant portal proteins were shown to form stable dodecameric rings except the variant W41A, which dissociated readily to monomers. Together, these results suggest that for P22 conserved tryptophan, residues in the wing domain of the portal protein play key roles in portal protein oligomerization and incorporation into procapsids, ultimately affecting the functionality of the portal protein at specific stages of virus assembly.

An overview of recent results obtained at the tokamak ASDEX Upgrade (AUG) is given. A work flow for predictive profile modelling of AUG discharges was established which is able to reproduce experimental H-mode plasma profiles based on engineering parameters only. In the plasma center, theoretical predictions on plasma current redistribution by a dynamo effect were confirmed experimentally. For core transport, the stabilizing effect of fast ion distributions on turbulent transport is shown to be important to explain the core isotope effect and improves the description of hollow low-Z impurity profiles. The L–H power threshold of hydrogen plasmas is not affected by small helium admixtures and it increases continuously from the deuterium to the hydrogen level when the hydrogen concentration is raised from 0 to 100%. One focus of recent campaigns was the search for a fusion relevant integrated plasma scenario without large edge localised modes (ELMs). Results from six different ELM-free confinement regimes are compared with respect to reactor relevance: ELM suppression by magnetic perturbation coils could be attributed to toroidally asymmetric turbulent fluctuations in the vicinity of the separatrix. Stable improved confinement mode plasma phases with a detached inner divertor were obtained using a feedback control of the plasma β. The enhanced Dα H-mode regime was extended to higher heating power by feedback controlled radiative cooling with argon. The quasi-coherent exhaust regime was developed into an integrated scenario at high heating power and energy confinement, with a detached divertor and without large ELMs. Small ELMs close to the separatrix lead to peeling-ballooning stability and quasi continuous power exhaust. Helium beam density fluctuation measurements confirm that transport close to the separatrix is important to achieve the different ELM-free regimes. Based on separatrix plasma parameters and interchange-drift-Alfvén turbulence, an analytic model was derived that reproduces the experimentally found important operational boundaries of the density limit and between L- and H-mode confinement. Feedback control for the X-point radiator (XPR) position was established as an important element for divertor detachment control. Stable and detached ELM-free phases with H-mode confinement quality were obtained when the XPR was moved 10 cm above the X-point. Investigations of the plasma in the future flexible snow-flake divertor of AUG by means of first SOLPS-ITER simulations with drifts activated predict beneficial detachment properties and the activation of an additional strike point by the drifts. This work has been carried out within the framework of the EUROfusion Consortium and has received funding from the Euratom research and training programme 2014–2018 and 2019–2020 under Grant Agreement No. 633053. The views and opinions expressed herein do not necessarily reflect those of the European Commission. Peer Reviewed "Article signat per més de 50 autors/es: U. Stroth, D. Aguiam, E. Alessi, C. Angioni, N. Arden, R. Arredondo Parra, V. Artigues, O. Asunta, M. Balden, V. Bandaru, A. Banon-Navarro, K. Behler, A. Bergmann, M. Bergmann, J. Bernardo, M. Bernert, A. Biancalani, R. Bielajew, R. Bilato, G. Birkenmeier, T. Blanken, V. Bobkov, A. Bock, T. Body, T. Bolzonella, N. Bonanomi, A. Bortolon, B. Böswirth, C. Bottereau, A. Bottino, H. van den Brand, M. Brenzke, S. Brezinsek, D. Brida, F. Brochard, C. Bruhn, J. Buchanan, A. Buhler, A. Burckhart, Y. Camenen, B. Cannas, P. Cano Megias, D. Carlton, M. Carr, P. Carvalho, C. Castaldo, M. Cavedon, C. Cazzaniga, C. Challis, A. Chankin, C. Cianfarani, F. Clairet, S. Coda, R. Coelho, J.W. Coenen, L. Colas, G. Conway, S. Costea, D. Coster, T. Cote, A.J. Creely, G. Croci, D.J. Cruz Zabala, G. Cseh, A. Czarnecka, I. Cziegler, O. D'Arcangelo, A. Dal Molin, P. David, C. Day, M. de Baar, P. de Marné, R. Delogu, S. Denk, P. Denner, A. Di Siena, J.J. Dominguez Palacios Durán, D. Dunai, A. Drenik, M. Dreval, R. Drube, M. Dunne, B.P. Duval, R. Dux, T. Eich, S. Elgeti, A. Encheva, K. Engelhardt, B. Erdös, I. Erofeev, B. Esposito, E. Fable, M. Faitsch, U. Fantz, M. Farnik, H. Faugel, F. Felici, O. Ficker, S. Fietz, A. Figueredo, R. Fischer, O. Ford, L. Frassinetti, M. Fröschle, G. Fuchert, J.C. Fuchs, H. Fünfgelder, S. Futatani, K. Galazka, J. Galdon-Quiroga, D. Gallart Escolà, A. Gallo10, Y. Gao11, S. Garavaglia3, M. Garcia Muñoz16, B. Geiger21, L. Giannone1, S. Gibson32, L. Gil2, E. Giovannozzi18, S. Glöggler1, M. Gobbin8, J. Gonzalez Martin, T. Goodman, G. Gorini, T. Görler, D. Gradic, G. Granucci, A. Gräter, H. Greuner, M. Griener, M. Groth, A. Gude, L. Guimarais, S. Günter, G. Haas, A.H. Hakola, C. Ham, T. Happel, N. den Harder, G. Harrer, J. Harrison, V. Hauer, T. Hayward-Schneider, B. Heinemann, T. Hellsten, S. Henderson, P. Hennequin, A. Herrmann, E. Heyn, F. Hitzler, J. Hobirk, K. Höfler, J.H. Holm, M. Hölzl, C. Hopf, L. Horvath, T. Höschen, A. Houben, A. Hubbard, A. Huber, K. Hunger, V. Igochine, M. Iliasova, T. Ilkei, K. Insulander Björk, C. Ionita-Schrittwieser, I. Ivanova-Stanik, W. Jacob, N. Jaksic, F. Janky, A. Jansen van Vuuren, A. Jardin, F. Jaulmes, F. Jenko, T. Jensen, E. Joffrin, A. Kallenbach, S. Kálvin, M. Kantor, A. Kappatou, O. Kardaun, J. Karhunen4, C.-P. Käsemann, S. Kasilov, A. Kendl, W. Kernbichler, E. Khilkevitch, A. Kirk, S. Kjer Hansen, V. Klevarova, G. Kocsis, M. Koleva, M. Komm, M. Kong, A. Krämer-Flecken, K. Krieger, A. Krivska, O. Kudlacek, T. Kurki-Suonio, B. Kurzan, B. Labit, K. Lackner, F. Laggner, A. Lahtinen, P.T. Lang, P. Lauber, N. Leuthold, L. Li, J. Likonen, O. Linder, B. Lipschultz, Y. Liu, A. Lohs, Z. Lu, T. Luda di Cortemiglia, N.C. Luhmann, T. Lunt, A. Lyssoivan, T. Maceina, J. Madsen, A. Magnanimo, H. Maier, J. Mailloux, R. Maingi, O. Maj, E. Maljaars, P. Manas, A. Mancini, A. Manhard, P. Mantica, M. Mantsinen, P. Manz, M. Maraschek, C. Marchetto, L. Marrelli, P. Martin, A. Martitsch, F. Matos, M. Mayer, M.-L. Mayoral, D. Mazon, P.J. McCarthy, R. McDermott, R. Merkel, A. Merle, D. Meshcheriakov, H. Meyer, D. Milanesio, P. Molina Cabrera, F. Monaco, M. Muraca, F. Nabais, V. Naulin, R. Nazikian, R.D. Nem, A. Nemes-Czopf, G. Neu, R. Neu, A.H. Nielsen, S.K. Nielsen, T. Nishizawa, M. Nocente, J.-M. Noterdaeme, I. Novikau, S. Nowak, M. Oberkofler, R. Ochoukov, J. Olsen, F. Orain, F. Palermo, O. Pan, G. Papp, I. Paradela Perez, A. Pau, G. Pautasso, C. Paz-Soldan, P. Petersson, P. Piovesan, C. Piron, U. Plank, B. Plaum, B. Plöck, V. Plyusnin, G. Pokol, E. Poli, L. Porte, T. Pütterich, M. Ramisch, J. Rasmussen, G. Ratta, S. Ratynskaia, G. Raupp, D. Réfy, M. Reich1, F. Reimold, D. Reiser, M. Reisner, D. Reiter, T. Ribeiro, R. Riedl, J. Riesch, D. Rittich, J.F. Rivero Rodriguez, G. Rocchi, P. Rodriguez-Fernandez, M. Rodriguez-Ramos, V. Rohde, G. Ronchi, A. Ross, M. Rott, M. Rubel, D.A. Ryan, F. Ryter, S. Saarelma, M. Salewski, A. Salmi, O. Samoylov, L. Sanchis Sanchez, J. Santos, O. Sauter, G. Schall, K. Schlüter, K. Schmid, O. Schmitz, P.A. Schneider, R. Schrittwieser, M. Schubert, C. Schuster, T. Schwarz-Selinger, J. Schweinzer, E. Seliunin, A. Shabbir, A. Shalpegin, S. Sharapov, U. Sheikh, A. Shevelev, G. Sias, M. Siccinio, B. Sieglin, A. Sigalov, A. Silva, C. Silva, D. Silvagni, J. Simpson, S. Sipilä, E. Smigelskis, A. Snicker, E. Solano, C. Sommariva, C. Sozzi, G. Spizzo, M. Spolaore, A. Stegmeir, M. Stejner, J. Stober, E. Strumberge1, G. Suarez Lopez, H.-J. Sun, W. Suttrop, E. Sytova, T. Szepesi, B. Tál, T. Tala, G. Tardini, M. Tardocchi, D. Terranova, M. Teschke, E. Thorén, W. Tierens, D. Told, W. Treutterer, G. Trevisan, E. Trier, M. Tripský, M. Usoltceva, M. Valisa, M. Valovic, M. van Zeeland, F. Vannini, B. Vanovac, P. Varela, S. Varoutis, N. Vianello, J. Vicente, G. Verdoolaege, T. Vierle, E. Viezzer, I. Voitsekhovitch, U. von Toussaint, D. Wagner, X. Wang, M. Weiland, A.E. White, M. Willensdorfer, B. Wiringer, M. Wischmeier, R. Wolf, E. Wolfrum, Q. Yang, Q. Yu, R. Zagórski, I. Zammuto, T. Zehetbauer, W. Zhang, W. Zholobenko, M. Zilker, A. Zito, H. Zohm, S. Zoletnik and the EUROfusion MST1 Team "

The additively manufactured titanium aluminide alloy TNM-B1 was characterized microstructurally and mechanically in the as-built and hot isostatically pressed (HIP) condition. Tensile and constant amplitude tests were performed at room temperature and 800 {\deg}C. Using fractographic SEM images, the fracture-inducing defect was identified. With the HIP, defect number and size could be reduced, increasing fatigue strength by 43% to 500 MPa. Using the model approaches of Murakami and Shiozawa, the fatigue life was correlated with the local stress intensity factor and could be described as function of the stress amplitude as well as the size and location of fracture-inducing defects., Comment: 24 pages, 10 figures, 2 tables

Scaffolding proteins (SPs) are required for the capsid shell assembly of many tailed double-stranded DNA bacteriophages, some archaeal viruses, herpesviruses, and adenoviruses. Despite their importance, only one high-resolution structure is available for SPs within procapsids. Here, we use the inherent size limit of NMR to identify mobile segments of the 303-residue phage P22 SP free in solution and when incorporated into a ∼23 MDa procapsid complex. Free SP gives NMR signals from its acidic N-terminus (residues 1–40) and basic C-terminus (residues 264–303), whereas NMR signals from the middle segment (residues 41–263) are missing because of intermediate conformational exchange on the NMR chemical shift timescale. When SP is incorporated into P22 procapsids, NMR signals from the C-terminal helix-turn-helix domain disappear because of binding to the procapsid interior. Signals from the N-terminal domain persist, indicating that this segment retains flexibility when bound to procapsids. The unstructured character of the N-terminus, coupled with its high content of negative charges, is likely important for dissociation and release of SP during the double-stranded DNA genome packaging step accompanying phage maturation.

Tailed, double-stranded DNA bacteriophages provide a well-characterized model system for the study of viral assembly, especially for herpesviruses and adenoviruses. A wealth of genetic, structural, and biochemical work has allowed for the development of assembly models and an understanding of the DNA packaging process. The portal complex is an essential player in all aspects of bacteriophage and herpesvirus assembly. Despite having low sequence similarity, portal structures across bacteriophages share the portal fold and maintain a conserved function. Due to their dynamic role, portal proteins are surprisingly plastic, and their conformations change for each stage of assembly. Because the maturation process is dependent on the portal protein, researchers have been working to validate this protein as a potential antiviral drug target. Here we review recent work on the role of portal complexes in capsid assembly, including DNA packaging, as well as portal ring assembly and incorporation and analysis of portal structures.

Tailed dsDNA bacteriophages and herpesviruses form capsids using coat proteins that have the HK97 fold. In these viruses, the coat proteins first assemble into procapsids, which subsequently mature during DNA packaging. Generally interactions between the coat protein E-loop of one subunit and the P-domain of an adjacent subunit help stabilize both capsomers and capsids. Based on a recent 3.3 Å cryo-EM structure of the bacteriophage P22 virion, E-loop amino acids E52, E59 and E72 were suggested to stabilize the capsid through intra-capsomer salt bridges with the P-domain residues R102, R109 and K118. The glutamic acid residues were each mutated to alanine to test this hypothesis. The substitutions resulted in a WT phenotype and did not destabilize capsids; rather, the alanine substituted coat proteins increased the stability of procapsids and virions. These results indicate that different types of interactions must be used between the E-loop and P-domain to stabilize phage P22 procapsids and virions.

ASDEX Upgrade is planning the installation of a pair of in-vessel coils in order to study alternative divertor configurations, like an X-divertor (XD) or a Snowflake (SF) in a machine with a high heating power compared to its size. Two designs for the technical realization of these coils are currently proposed, one including z-shaped joints and one with a single spiral conductor. The magnetic fields produced by these conductors intrinsically have a non-axisymmetric component. In particular in the XD configuration, where very shallow field line incidence angles occur, these 3D fields have a strong impact on the power distribution on the outer divertor plate. The 2D and 3D plasma transport is studied by the SOLPS and initial EMC3-EIRENE code simulations, respectively, in order to support the decision making processes of the engineering design. Although several aspects still require further attention, this paper gives a status report. The strong toroidal asymmetries observed in the power deposition pattern for the spiral conductor seem to be strongly reduced, when highly dissipative divertor conditions are reached. The asymmetry for the z-joint design is substantially smaller than the spiral conductor even for low-dissipative conditions. Keywords: Power exhaust, Alternative divertor, ASDEX upgrade, EMC3-EIRENE, Tokamak, X-divertor

The imaging heavy ion beam probe (i-HIBP) is a new diagnostic concept realized at the tokamak ASDEX Upgrade (AUG) in order to obtain two-dimensional information about the density, the magnetic field and the electrostatic potential at the plasma edge. Although the two main components of the i-HIBP, an alkali beam based injector and a scintillator based detector, involve well-developed technologies, further developments were necessary to realize the i-HIBP at AUG. In dedicated laboratory tests, a new type of cesium source was characterized and the neutralization efficiency and properties of the primary cesium beam were found to be similar to alkali beams made of lighter elements. The use of cesium had also impact on the choice of the scintillator material, which was experimentally investigated in terms of photon yield, energy dependence and degradation revealing significant differences under irradiation with cesium ions compared to irradiation with hydrogenic beams. Due to constrictions of the AUG experiment setup, the high voltage components, the in-vessel shutter technology and the maintenance capabilities of the i-HIBP required new developments for the commissioning of the diagnostic., This work received funding from the Helmholtz Association under grant no. VH-NG-1350. This work received funding from the European Research Council (ERC) under the European Union’s Horizon 2020 research and innovation programme (grant agreement No. 805162). This work has been carried out within the framework of the EUROfusion Consortium and has received funding from the Euratom research and training programme 2014–2018 and 2019–2020 under grant agreement No 633053. The views and opinions expressed herein do not necessarily reflect those of the European Commission.

A physics and engineering analysis of alternative divertor configurations is carried out by examining benefits and problems by comparing the baseline single null solution with a Snowflake, an X- and a Super-X divertor. It is observed that alternative configurations can provide margin and resilience against large power fluctuations, but their engineering has intrinsic difficulties, especially in the balance between structural solidity and accessibility of the components and when the specific poloidal field coil positioning poses further constraints. A hybrid between the X- and Super-X divertor is proposed as a possible solution to the integration challenge.

There is proposed a new upper divertor for the A SDEX U p g rade (AUG) tokamak experiment [1] . It is planned to be equipped with internal coils for investigation of advanced magnetic configurations like e.g. „snowflake“ [2] . Due to the close vicinity of the coils to the plasma, high induced and very stiff voltages are expected during disruption events, as shown in [ 3 , 4 ],. This voltage is a high risk for either damaging the connected power supplies and/or for turning into high currents causing damage to the tokamak by Lorentz forces. The proposed device named “ripping crowbar” detects and overtakes the full high voltage of up to 5 kV during a plasma disruption at full load current of up to 3 kA to protect the connected power supply which can deal with voltage not higher than 340 V absolute value. The concept will be given and discussed. Experiments were started at much lower current and voltage by use of commercially available hardware. This is a starting point to enhance the working regime in a time-saving way, because there exist no commercially available solution for the target values. The only known field with comparable power stage solutions can be found in the field of H igh V oltage D irect C urrent (HVDC) circuit breakers [5] . The final solution should be scalable in voltage, current and power to adapt it to other applications in and outside the field of fusion technology. Part of the development are the I nsulated G ate B ipolar T ransistor (IGBT) based powerstage, the drivers, the measurement unit to detect disruptions and the triggering unit. At the end, most important will be reliability of this safety relevant device to protect multi-million investments into power supply and new divertor.

ASDEX Upgrade (AUG) electrical power is provided with three Flywheel Generators (FGs) that are charged up before the start of each plasma pulse with 15 MW for 30 minutes. The stored energy is then used to satisfy the high power needs during the pulse of up to 400 MW. The biggest FG (‘EZ2’) in case of a major fault could not be replaced by any other FG of such size because no comparable devices are available on the free market. Therefore, the development of an alternative energy storage with high power and energy density and fully controllable output is planned. Supercapacitors (SCs) are well known for their high specific power. The combination of this technology and a proper power converter topology such as the Modular Multilevel Converter (MMC) represent a promising alternative to be explored to replace Tokamaks FGs. The MMC topology allows a discrete-leveled output voltage and, thanks to its high cells number, it can operate continuously even in case of fault of some cells, while a FG could not. In this paper the concept of a SCs-based power supply for AUG's Toroidal Field (TF) Coils is presented, highlighting the main advantages and challenges of this project.

ASDEX Upgrade will be evolved by installing a new upper divertor with two in-vessel coils allowing the investigation of alternative magnetic configurations. The in-vessel coils will be bended inside the torus. The co-axial conductor consists of a Tefzel insulated water cooled copper core embedded into a stainless steel protection shield. To test the conductor concept and to qualify the electrical and thermal properties of the Tefzel insulated conductor (TIC), prototype conductors of 3 and 8 m length were used. These conductors undergo electrical and thermal tests accompanied by FEM calculations. The electrical tests include high voltage and partial discharge tests. For thermo-mechanical tests the prototype conductors were fed with up to 13 kA for 5 s. During the test the copper conductor was heated up by 60 K. The Tefzel cladding and the protection tube are warmed up with a delay given by the thermal heat conduction and capacity. The thermo-mechanical behaviour of the TIC during the heating and cooling phase could be confirmed by the FEM-models. As part of the qualification, the conductor was thermally overloaded by a factor of 3, without degradation. The paper presents the electrical and thermal tests as well as the results of the related FEM calculations.

Phage L encodes a trimeric 43 kDa decoration protein (Dec) that noncovalently binds and stabilizes the capsids of the homologous phages L and P22 in vitro. At physiological pH Dec was unsuitable for NMR. We were able to obtain samples amenable for NMR spectroscopy by unfolding Dec to pH 2 and refolding it to pH 4. Our unfolding/refolding protocol con verted trimeric Dec to a folded 14.4 kDa monomer. We verified that the acid-unfolding protocol did not perturb the secondary structure, or the capsid-binding function of refolded Dec. We were able to obtain complete (1)H, (15)N, and (13)C assignments for the Dec monomer, as well as information on its secondary structure and dynamics based on chemical shift assignments. The assigned NMR spectrum is being used to determine the three-dimensional structure of Dec, which is important for understanding how the trimer binds phage capsids and for the use of the protein as a platform for phage-display nanotechnology.

Tailed double-stranded DNA bacteriophages inject some proteins with their dsDNA during infection. Phage P22 injects about 12, 12, and 30 molecules of the proteins encoded by genes 7, 16 and 20, respectively. After their ejection from the virion, they assemble into a trans-periplasmic conduit through which the DNA passes to enter the cytoplasm. The location of these proteins in the virion before injection is not well understood, although we recently showed they reside near the portal protein barrel in DNA-filled heads. In this report we show that when these proteins are missing from the virion, a longer than normal DNA molecule is encapsidated by the P22 headful DNA packaging machinery. Thus, the ejection proteins occupy positions within the virion that can be occupied by packaged DNA when they are absent.

For the nuclear fusion experiment ASDEX Upgrade (AUG) an inverter system to individually feed the 16 in-vessel saddle coils was built. After an operating phase with four inverters that supplied groups of up to 4 coils connected in series, now the full system is working. The common DC-link is fed by an existing current-mode thyristor rectifier. The idea was to use the thyristor rectifier in voltage control mode. Therefore the control system and the power stack had to be adjusted. This publication describes the modifications made to the thyristor rectifier in order to feed a DC-link and stabilize its voltage under all load conditions. Also the integrated safety systems are shown.

dsDNA tailed phages and herpesviruses assemble their capsids using coat proteins that have the ubiquitous HK97 fold. Though this fold is common, we do not have a thorough understanding of the different ways viruses adapt it to maintain stability in various environments. The HK97-fold E-loop, which connects adjacent subunits at the outer periphery of capsomers, has been implicated in capsid stability. Here we show that in bacteriophage P22, residue W61 at the tip of the E-loop plays a role in stabilizing procapsids and in maturation. We hypothesize that a hydrophobic pocket is formed by residues I366 and W410 in the P-domain of a neighboring subunit within a capsomer, into which W61 fits like a peg. In addition, W61 likely bridges to residues A91 and L401 in P-domain loops of an adjacent capsomer, thereby linking the entire capsid together with a network of hydrophobic interactions. There is conservation of this hydrophobic network in the distantly related P22-like phages, indicating that this structural feature is likely important for stabilizing this family of phages. Thus, our data shed light on one of the varied elegant mechanisms used in nature to consistently build stable viral genome containers through subtle adaptation of the HK97 fold.IMPORTANCESimilarities in assembly reactions and coat protein structures of the dsDNA tailed phages and herpesviruses make phages ideal models to understand capsid assembly and identify potential targets for antiviral drug discovery. The coat protein E-loops of these viruses are involved in both intra-and intercapsomer interactions. In phage P22, hydrophobic interactions peg the coat protein subunits together within a capsomer, where the E-loop hydrophobic residue W61 of one subunit packs into a pocket of hydrophobic residues I366 and W410 of the adjacent subunit. W61 also makes hydrophobic interactions with A91 and L401 of a subunit in an adjacent capsomer. We show these intra-and intercapsomer hydrophobic interactions form a network crucial to capsid stability and proper assembly.

Tailed double-stranded DNA (dsDNA) bacteriophages, herpesviruses, and adenoviruses package their genetic material into a precursor capsid through a dodecameric ring complex called the portal protein, which is located at a unique 5-fold vertex. In several phages and viruses, including T4, Φ29, and herpes simplex virus 1 (HSV-1), the portal forms a nucleation complex with scaffolding proteins (SPs) to initiate procapsid (PC) assembly, thereby ensuring incorporation of only one portal ring per capsid. However, for bacteriophage P22, the role of its portal protein in initiation of procapsid assembly is unclear. We have developed an in vitro P22 assembly assay where portal protein is coassembled into procapsid-like particles (PLPs). Scaffolding protein also catalyzes oligomerization of monomeric portal protein into dodecameric rings, possibly forming a scaffolding protein-portal protein nucleation complex that results in one portal ring per P22 procapsid. Here, we present evidence substantiating that the P22 portal protein, similarly to those of other dsDNA viruses, can act as an assembly nucleator. The presence of the P22 portal protein is shown to increase the rate of particle assembly and contribute to proper morphology of the assembled particles. Our results highlight a key function of portal protein as an assembly initiator, a feature that is likely conserved among these classes of dsDNA viruses. IMPORTANCE The existence of a single portal ring is essential to the formation of infectious virions in the tailed double-stranded DNA (dsDNA) phages, herpesviruses, and adenoviruses and, as such, is a viable antiviral therapeutic target. How only one portal is selectively incorporated at a unique vertex is unclear. In many dsDNA viruses and phages, the portal protein acts as an assembly nucleator. However, early work on phage P22 assembly in vivo indicated that the portal protein did not function as a nucleator for procapsid (PC) assembly, leading to the suggestion that P22 uses a unique mechanism for portal incorporation. Here, we show that portal protein nucleates assembly of P22 procapsid-like particles (PLPs). Addition of portal rings to an assembly reaction increases the rate of formation and yield of particles and corrects improper particle morphology. Our data suggest that procapsid assembly may universally initiate with a nucleation complex composed minimally of portal and scaffolding proteins (SPs).

Despite very low sequence homology, the major capsid proteins of double-stranded DNA (dsDNA) bacteriophages, some archaeal viruses, and the herpesviruses share a structural motif, the HK97 fold. Bacteriophage P22, a paradigm for this class of viruses, belongs to a phage gene cluster that contains three homology groups: P22-like, CUS-3-like, and Sf6-like. The coat protein of each phage has an inserted domain (I-domain) that is more conserved than the rest of the coat protein. In P22, loops in the I-domain are critical for stabilizing intra- and intersubunit contacts that guide proper capsid assembly. The nuclear magnetic resonance (NMR) structures of the P22, CUS-3, and Sf6 I-domains reveal that they are all six-stranded, anti-parallel β-barrels. Nevertheless, significant structural differences occur in loops connecting the β-strands, in surface electrostatics used to dock the I-domains with their respective coat protein core partners, and in sequence motifs displayed on the capsid surfaces. Our data highlight the structural diversity of I-domains that could lead to variations in capsid assembly mechanisms and capsid surfaces adapted for specific phage functions. IMPORTANCE Comparative studies of protein structures often provide insights into their evolution. The HK97 fold is a structural motif used to form the coat protein shells that encapsidate the genomes of many dsDNA phages and viruses. The structure and function of coat proteins based on the HK97 fold are often embellished by the incorporation of I-domains. In the present work we compare I-domains from three phages representative of highly divergent P22-like homology groups. While the three I-domains share a six-stranded β-barrel skeleton, there are differences (i) in structure elements at the periphery of the conserved fold, (ii) in the locations of disordered loops important in capsid assembly and conformational transitions, (iii) in surfaces charges, and (iv) in sequence motifs that are potential ligand-binding sites. These structural modifications on the rudimentary I-domain fold suggest that considerable structural adaptability was needed to fulfill the versatile range of functional requirements for distinct phages.

dsDNA Bacteriophages, some dsDNA archaeal viruses and the Herpesviruses share many features including a common capsid assembly pathway and coat protein fold. The coat proteins of these viruses, which have the HK97 fold, co-assemble with a free or attached scaffolding protein and other capsid proteins into a precursor capsid, known as a procapsid or prohead. The procapsid is a metastable state that increases in stability as a result of morphological changes that occur during the dsDNA packaging reaction. We review evidence from several systems indicating that proper contacts acquired in the assembly of the procapsid are critical to forming the correct morphology in the mature capsid.

SummaryScaffolding proteins are requisite for the capsid shell assembly of many tailed dsDNA bacteriophages, some archaeal viruses, herpesviruses, and adenoviruses. Despite their importance, no high-resolution structural information is available for scaffolding proteins within capsids. Here we use the inherent size limit of NMR to identify mobile segments of the phage P22 scaffolding protein in solution and when incorporated into a ~23 MDa procapsid complex. Free scaffolding protein gives NMR signals from both the N and C-terminus. When scaffolding protein is incorporated into P22 procapsids, NMR signals from the C-terminal helix-turn-helix (HTH) domain disappear due to binding to the procapsid interior. Signals from the N-terminal domain persist, indicating this segment retains flexibility when bound to procapsids. The unstructured character of the N-terminus coupled with its high content of negative charges, is likely important for the dissociation and release of scaffolding protein, during the genome packaging step accompanying phage maturation.Graphical AbstractScaffolding protein (SP) nucleates the assembly of phage P22 coat proteins into an icosahedral capsid structure that envelops the viral genome. NMR spectra of free SP show signals from the N-terminus (red) and a helix-turn-helix domain at the C-terminus (blue). When SP is incorporated into empty phage P22 procapsids to form a 23 MDa complex, the subset of signals from the N-terminal 40 residues persist indicating this segment is disordered. The unfolded nature of the N-terminus coupled with its negatively charged character, is important for the functional requirement of SP to exit the capsid as it becomes packaged with its genome.

The poloidal distribution of electromagnetic loads during fast transients in the vacuum vessel of COMPASS-U tokamak is calculated analytically. The estimates are then compared with CarMa0NL numerical simulations. The results show that the poloidal eddy currents in the vacuum vessel must be taken into account for the proper evaluation of disruption forces in the COMPASS-U tokamak.

The design and optimization of a future tokamak fusion reactor, from the point of view of the plasma performance and output fusion power, requires the understanding of the underlying physics and the validation on present experiments of the theory-based tools used for the predictions. Present experimental efforts are devoted to approach reactor-relevant parameters (collisionality, , normalized heat fluxes and sources, temperatures ratio) as much as possible. In this work a series of discharges performed on ASDEX Upgrade are presented, where plasma density and auxiliary power levels are scanned to cover a parameter space that moves towards reactor relevant parameters. On this dedicated discharge dataset, a first-principle-based model is then applied for validation. The degree of agreement between code results and experimental measurements is shown and discussed. In cases where discrepancy is found, possible causes are identified. It is shown that the employed modeling tool can predict the overall trend, consistent with more fundamental theoretical considerations, although quantitative extrapolation still has to be performed with care. Key results of this work show that the density peaking is mainly sustained by turbulence, with a minor role for the fueling source, and how this experimental demonstration is important to predict future reactor density profiles. Moreover, the role of electromagnetic effects is also pointed out.

ASDEX Upgrade is a tokamak that can be operated with the strike lines in the upper and/or the lower divertor. In 2016 a project was started to develop and install a new upper divertor with internal coils and an in-vessel cryo-pump. The aim is to investigate alternative magnetic configurations that may facilitate the access to detachment via an enhanced poloidal flux tube expansion and/or connection length. To realize the envisaged magnetic configurations two internal coils operated with up to 52 kAt will be installed near the upper outer strike line. Since the conceptual design was presented critical aspects of the project were identified and investigated in detail. These are the vessel integration, the coil concept, the forces, in particular during disruptions, an intrinsic safe power supply, the cryo-pump and last but not least, operation with co and counter magnetic field. The present status of each of the components is presented in the paper.

A new upper divertor is proposed for the ASDEX Upgrade (AUG) tokamak experiment. It is planned to be equipped with internal coils for investigation of alternative magnetic configurations like e.g. “snowflake” (Herrmann et al., 2017 [ 1 ]). Since the coils are close to the plasma, high induced and very stiff voltages are expected during disruption events. Because only very vague analytical estimates of voltages, forces and coupling factors were available, an improvement by the help of Finite Element Method (FEM) was envisaged. Therefore, recorded measurements of currents, plasma position, plasma profile and the geometry were integrated in an electromagnetic simulation as boundary conditions to calculate resulting field distributions during selected AUG disruptions. The time resolution can be better than 100 μs and the required computing resources are comparably small due to the assumption of 2D axis-symmetry. The results were compared with magnetic probe measurements integrated into the tokamak ultimately observing good agreement. After this, the FE model was modified including the new divertor to calculate all relevant parameters. The output of these calculations has strong implications for the coil and power supply design: i) The power supply will be protected by a new kind of crowbar to avoid damage of the power supply due to overvoltage and uncontrolled current and force rise of the coils. The concept of this so called “ripping crowbar” is introduced, which is now under development. ii) The coil cable should be coaxial shaped to monitor isolation faults and to become inherently safe against single-turn shortcuts, identified as destructive fault scenario.

The major coat proteins of dsDNA tailed phages and herpesviruses form capsids by a mechanism that includes active packaging of the dsDNA genome into a precursor procapsid, followed by expansion and stabilization of the capsid. These viruses have evolved diverse strategies to fortify their capsids, such as non-covalent binding of auxiliary “decoration” (Dec) proteins. The Dec protein from the P22-like phage L has a highly unusual binding strategy that precisely distinguishes between nearly identical three-fold and quasi-three-fold sites of the icosahedral capsid. Cryo-electron microscopy and three-dimensional image reconstruction were employed to determine the structure of native phage L particles. NMR was used to determine the structure/dynamics of Dec in solution. Lastly, the NMR structure and the cryo-EM density envelope were combined to build a model of the capsid-bound Dec trimer. Key regions that modulate the binding interface were verified by site-directed mutagenesis.

The copepod Calanus finmarchicus plays a crucial role in the north Atlantic food web. Its seasonal life cycle involves reproduction and development in surface waters before overwintering in diapause at depth. Although diapause has been studied for more than a century, the factors responsible for the initiation and termination of it are still unclear. Endogenous clocks have been identified as potent tools for photoperiod measurement and seasonal rhythmicity in many terrestrial species, but knowledge of these remains scarce in the marine realm. Focusing on the dominant CV copepodid stage, we sampled a population of C. finmarchicus from a Scottish sea loch to characterize population dynamics, several physiological parameters, and diel and seasonal expression rhythms of 35 genes representing different metabolic pathways, including the circadian clock machinery. This generated a detailed overview of the seasonal cycle of C. finmarchicus including the most extensive field dataset on circadian clock gene expression in a marine species to date. Gene expression patterns revealed distinct gene clusters upregulated at different phases of the copepod’s seasonal cycle. While diel clock cycling was restricted to the active spring/summer phase, many clock genes exhibited the highest expression during diapause. Our results provide new insights into diapause on physiological and genetic levels. We suggest that photoperiod, in interaction with internal and external factors (lipid content, temperature, food availability) and the endogenous clock mechanism, plays an important role in the timing of diapause in C. finmarchicus.

The ASDEX Upgrade (AUG) programme, jointly run with the EUROfusion MST1 task force, continues to significantly enhance the physics base of ITER and DEMO. Here, the full tungsten wall is a key asset for extrapolating to future devices. The high overall heating power, flexible heating mix and comprehensive diagnostic set allows studies ranging from mimicking the scrape-off-layer and divertor conditions of ITER and DEMO at high density to fully non-inductive operation (q95 = 5.5, ) at low density. Higher installed electron cyclotron resonance heating power 6 MW, new diagnostics and improved analysis techniques have further enhanced the capabilities of AUG. Stable high-density H-modes with MW m−1 with fully detached strike-points have been demonstrated. The ballooning instability close to the separatrix has been identified as a potential cause leading to the H-mode density limit and is also found to play an important role for the access to small edge-localized modes (ELMs). Density limit disruptions have been successfully avoided using a path-oriented approach to disruption handling and progress has been made in understanding the dissipation and avoidance of runaway electron beams. ELM suppression with resonant magnetic perturbations is now routinely achieved reaching transiently . This gives new insight into the field penetration physics, in particular with respect to plasma flows. Modelling agrees well with plasma response measurements and a helically localised ballooning structure observed prior to the ELM is evidence for the changed edge stability due to the magnetic perturbations. The impact of 3D perturbations on heat load patterns and fast-ion losses have been further elaborated. Progress has also been made in understanding the ELM cycle itself. Here, new fast measurements of and Er allow for inter ELM transport analysis confirming that Er is dominated by the diamagnetic term even for fast timescales. New analysis techniques allow detailed comparison of the ELM crash and are in good agreement with nonlinear MHD modelling. The observation of accelerated ions during the ELM crash can be seen as evidence for the reconnection during the ELM. As type-I ELMs (even mitigated) are likely not a viable operational regime in DEMO studies of 'natural' no ELM regimes have been extended. Stable I-modes up to have been characterised using -feedback. Core physics has been advanced by more detailed characterisation of the turbulence with new measurements such as the eddy tilt angle—measured for the first time—or the cross-phase angle of and fluctuations. These new data put strong constraints on gyro-kinetic turbulence modelling. In addition, carefully executed studies in different main species (H, D and He) and with different heating mixes highlight the importance of the collisional energy exchange for interpreting energy confinement. A new regime with a hollow profile now gives access to regimes mimicking aspects of burning plasma conditions and lead to nonlinear interactions of energetic particle modes despite the sub-Alfvénic beam energy. This will help to validate the fast-ion codes for predicting ITER and DEMO. This work has been carried out within the framework of the EUROfusion Consortium and has received funding from the Euratom research and training programme 2014–2018 and 2019–2020 under grant agreement No. 633053. The views and opinions expressed herein do not necessarily reflect those of the European Commission. "Article signat per més de 100 autors/es: H. Meyer, for the AUG Team: D. Aguiam, C. Angioni, C.G. Albert, N. Arden, R. Arredondo Parra, O. Asunta, M. de Baar, M. Balden, V. Bandaru, K. Behler, A. Bergmann, J. Bernardo, M. Bernert, A. Biancalani, R. Bilato, G. Birkenmeier, T.C. Blanken, V. Bobkov, A. Bock, T. Bolzonella, A. Bortolon, B. Böswirth, C. Bottereau, A. Bottino, H. van den Brand, S. Brezinsek, D. Brida, F. Brochard, C. Bruhn, J. Buchanan, A. Buhler, A. Burckhart, Y. Camenen, D. Carlton, M. Carr, D. Carralero, C. Castaldo, M. Cavedon, C. Cazzaniga, S. Ceccuzzi, C. Challis, A. Chankin, S. Chapman, C. Cianfarani, F. Clairet, S. Coda, R. Coelho, J.W. Coenen, L. Colas, G.D. Conway, S. Costea, D.P. Coster, T.B. Cote, A. Creely, G. Croci, G. Cseh, A. Czarnecka, I. Cziegler, O. D'Arcangelo, P. David, C. Day, R. Delogu, P. de Marné, S.S. Denk, P. Denner, M. Dibon, A. Di Siena, D. Douai, A. Drenik, R. Drube, M. Dunne, B.P. Duval, R. Dux, T. Eich, S. Elgeti, K. Engelhardt, B. Erdös, I. Erofeev, B. Esposito, E. Fable, M. Faitsch, U. Fantz, H. Faugel, I. Faust, F. Felici, J. Ferreira, S. Fietz, A. Figuereido, R. Fischer, O. Ford, L. Frassinetti, S. Freethy, M. Fröschle, G. Fuchert, J.C. Fuchs, H. Fünfgelder, K. Galazka, J. Galdon-Quiroga, A. Gallo, Y. Gao, S. Garavaglia, A. Garcia-Carrasco, M. Garcia-Muñoz, B. Geiger, L. Giannone, L. Gil, E. Giovannozzi, C. Gleason-González, S. Glöggler, M. Gobbin, T. Görler, I. Gomez Ortiz, J. Gonzalez Martin, T. Goodman, G. Gorini, D. Gradic, A. Gräter, G. Granucci, H. Greuner, M. Griener, M. Groth, A. Gude, S. Günter, L. Guimarais, G. Haas, A.H. Hakola, C. Ham, T. Happel, N. den Harder, G.F. Harrer, J. Harrison, V. Hauer, T. Hayward-Schneider, C.C. Hegna, B. Heinemann, S. Heinzel, T. Hellsten, S. Henderson, P. Hennequin, A. Herrmann, M.F. Heyn, E. Heyn, F. Hitzler, J. Hobirk, K. Höfler, M. Hölzl, T. Höschen, J.H. Holm, C. Hopf, W.A. Hornsby, L. Horvath, A. Houben, A. Huber, V. Igochine, T. Ilkei, I. Ivanova-Stanik, W. Jacob, A.S. Jacobsen, F. Janky, A. Jansen van Vuuren, A. Jardin, F. Jaulmes, F. Jenko, T. Jensen, E. Joffrin, C.-P. Käsemann, A. Kallenbach, S. Kálvin, M. Kantor, A. Kappatou, O. Kardaun, J. Karhunen, S. Kasilov,, Y. Kazakov, W. Kernbichler, A. Kirk, S. Kjer Hansen, V. Klevarova, G. Kocsis, A. Köhn, M. Koubiti, K. Krieger, A. Krivska, A. Krämer-Flecken, O. Kudlacek, T. Kurki-Suonio, B. Kurzan, B. Labit, K. Lackner, F. Laggner, P.T. Lang, P. Lauber, A. Lebschy, N. Leuthold, M. Li, O. Linder, B. Lipschultz, F. Liu, Y. Liu, A. Lohs, Z. Lu, T. Luda di Cortemiglia, N.C. Luhmann, R. Lunsford, T. Lunt, A. Lyssoivan, T. Maceina, J. Madsen, R. Maggiora, H. Maier, O. Maj, J. Mailloux, R. Maingi, E. Maljaars, P. Manas, A. Mancini, A. Manhard, M.-E. Manso, P. Mantica, M. Mantsinen, P. Manz, M. Maraschek, C. Martens, P. Martin, L. Marrelli, A. Martitsch, M. Mayer, D. Mazon, P.J. McCarthy, R. McDermott, H. Meister, A. Medvedeva, R. Merkel, A. Merle, V. Mertens, D. Meshcheriakov, O. Meyer, J. Miettunen, D. Milanesio, F. Mink, A. Mlynek, F. Monaco, C. Moon, F. Nabais, A. Nemes-Czopf, G. Neu, R. Neu, A.H. Nielsen, S.K. Nielsen, V. Nikolaeva, M. Nocente, J.-M. Noterdaeme, I. Novikau, S. Nowak, M. Oberkofler, M. Oberparleiter, R. Ochoukov, T. Odstrcil, J. Olsen, F. Orain, F. Palermo, O. Pan, G. Papp, I. Paradela Perez, A. Pau, G. Pautasso, F. Penzel, P. Petersson, J. Pinzón Acosta, P. Piovesan, C. Piron, R. Pitts, U. Plank, B. Plaum, B. Ploeckl, V. Plyusnin, G. Pokol, E. Poli, L. Porte, S. Potzel, D. Prisiazhniuk, T. Pütterich, M. Ramisch, J. Rasmussen, G.A. Rattá, S. Ratynskaia, G. Raupp, G.L. Ravera, D. Réfy, M. Reich, F. Reimold, D. Reiser, T. Ribeiro, J. Riesch, R. Riedl, D. Rittich, J.F. Rivero-Rodriguez, G. Rocchi, M. Rodriguez-Ramos, V. Rohde, A. Ross1, M. Rott, M. Rubel, D. Ryan, F. Ryter, S. Saarelma, M. Salewski, A. Salmi, L. Sanchis-Sanchez, J. Santos, O. Sauter, A. Scarabosio, G. Schall, K. Schmid, O. Schmitz, P.A. Schneider, R. Schrittwieser, M. Schubert, T. Schwarz-Selinger, J. Schweinzer, B. Scott, T. Semer, E. Seliunin, M. Sertoli, A. Shabbir, A. Shalpegin, L. Shao, S. Sharapov, G. Sias, M. Siccinio, B. Sieglin, A. Sigalov, A. Silva, C. Silva, D. Silvagni, P. Simon, J. Simpson, E. Smigelskis, A. Snicker, C. Sommariva, C. Sozzi, M. Spolaore, A. Stegmeir, M. Stejner, J. Stober, U. Stroth, E. Strumberger, G. Suarez, H.-J. Sun, W. Suttrop, E. Sytova, T. Szepesi, B. Tál, T. Tala, G. Tardini, M. Tardocchi, M. Teschke, D. Terranova, W. Tierens, E. Thorén, D. Told, P. Tolias, O. Tudisco, W. Treutterer, E. Trier, M. Tripský, M. Valisa, M. Valovic, B. Vanovac, D. van Vugt, S. Varoutis, G. Verdoolaege, N. Vianello, J. Vicente, T. Vierle, E. Viezzer, U. von Toussaint, D. Wagner, N. Wang, X. Wang, M. Weiland, A.E. White, S. Wiesen, M. Willensdorfer, B. Wiringer, M. Wischmeier, R. Wolf, E. Wolfrum, L. Xiang, Q. Yang, Z. Yang, Q. Yu, R. Zagórski, I. Zammuto, W. Zhang, M. van Zeeland, T. Zehetbauer, M. Zilker, S. Zoletnik, H. Zohm and the EUROfusion MST1 Team55

For many (if not all) bacterial and archaeal tailed viruses and eukaryotic Herpesvirdae the HK97-fold serves as the major architectural element in icosahedral capsid formation while still enabling the conformational flexibility required during assembly and maturation. Auxiliary proteins or Δ-domains strictly control assembly of multiple, identical, HK97-like subunits into procapsids with specific icosahedral symmetries, rather than aberrant non-icosahedral structures. Procapsids are precursor structures that mature into capsids in a process involving release of auxiliary proteins (or cleavage of Δ-domains), dsDNA packaging, and conformational rearrangement of the HK97-like subunits. Some coat proteins built on the ubiquitous HK97-fold also have accessory domains or loops that impart specific functions, such as increased monomer, procapsid, or capsid stability. In this review, we analyze the numerous HK97-like coat protein structures that are emerging in the literature (over 40 at time of writing) by comparing their topology, additional domains, and their assembly and misassembly reactions.

The P22 bacteriophage group is a subgroup of the λ phage supercluster, comprised of the three major sequence types Sf6, P22, and CUS-3, based on their capsid proteins. Our goal is to investigate the extent to which structure–function relationships are conserved for the viral coat proteins and I-domains in this subgroup. Sf6 is a phage that infects the human pathogen Shigella flexneri. The coat protein of Sf6 assembles into a procapsid, which further undergoes maturation during DNA packaging into an infectious virion. The Sf6 coat protein contains a genetically inserted domain, termed the I-domain, similar to the ones present in the P22 and CUS-3 coat proteins. Based on the P22 example, I-domains play important functional roles in capsid assembly, stability, viability, and size-determination. Here we report the 1H, 15N, and 13C chemical shift assignments for the I-domain of the Sf6 phage coat protein. Chemical shift-based secondary structure prediction and hydrogen-bond patterns from a long-range HNCO experiment indicate that the Sf6 I-domain adopts a 6-stranded β-barrel fold like those of P22 and CUS-3 but with important differences, including the absence of the D-loop that is critical for capsid assembly and the addition of a novel disordered loop region.

Im Beschwerdekomplex um das Kiefergelenk wird grundsatzlich zwischen Funktionsstorung und Erkrankung unterschieden. Wahrend sich viele Funktionsstorungen konservativ behandeln lassen, stellt eine Kiefergelenkerkrankung haufig eine Indikation zur Operation dar. Die Aufgabe des MKG-Chirurgen besteht darin, die Patienten herauszufiltern, die einer chirurgischen Therapie zuganglich sind und die von ihr auch dauerhaft profitieren konnen. Den nicht chirurgisch zu behandelnden Patienten sollte der Weg einer weiteren Diagnostik und Therapie, auch in anderen Disziplinen, aufgezeigt werden. Der vorliegende Beitrag beschreibt die Symptome und Diagnostik der einzelnen Krankheitsbilder und zeigt die jeweiligen Therapiemoglichkeiten auf.

A novel role for scaffolding protein in portal ring formation., Most double-stranded DNA viruses package genetic material into empty precursor capsids (or procapsids) through a dodecameric portal protein complex that occupies 1 of the 12 vertices of the icosahedral lattice. Inhibiting incorporation of the portal complex prevents the formation of infectious virions, making this step an excellent target for antiviral drugs. The mechanism by which a sole portal assembly is selectively incorporated at the special vertex is unclear. We recently showed that, as part of the DNA packaging process for bacteriophage P22, the dodecameric procapsid portal changes conformation to a mature virion state. We report that preformed dodecameric rings of P22 portal protein, as opposed to portal monomers, incorporate into nascent procapsids, with preference for the procapsid portal conformation. Finally, a novel role for P22 scaffolding protein in triggering portal ring formation from portal monomers is elucidated and validated by incorporating de novo assembled portal rings into procapsids.

Tailed bacteriophages and herpesviruses assemble infectious particles via an empty precursor capsid (or ‘procapsid') built by multiple copies of coat and scaffolding protein and by one dodecameric portal protein. Genome packaging triggers rearrangement of the coat protein and release of scaffolding protein, resulting in dramatic procapsid lattice expansion. Here, we provide structural evidence that the portal protein of the bacteriophage P22 exists in two distinct dodecameric conformations: an asymmetric assembly in the procapsid (PC-portal) that is competent for high affinity binding to the large terminase packaging protein, and a symmetric ring in the mature virion (MV-portal) that has negligible affinity for the packaging motor. Modelling studies indicate the structure of PC-portal is incompatible with DNA coaxially spooled around the portal vertex, suggesting that newly packaged DNA triggers the switch from PC- to MV-conformation. Thus, we propose the signal for termination of ‘Headful Packaging' is a DNA-dependent symmetrization of portal protein., Tailed bacteriophages assemble empty precursor capsids known as procapsids that are subsequently filled with viral DNA by a genome-packaging motor. Here the authors present a structure-based analysis that suggests the signal for termination of genome packaging is achieved through a DNA-dependent symmetrization of portal protein.

The generated magnetic field of 16 coils for the control of magneto-hydrodynamic instabilities (1.3 kA each, 500 Hz bandwidth) installed into the nuclear fusion experiment ASDEX Upgrade have to be freely adjustable in space and time. Therefore, a 16-phases, fast-switching IGBT-based inverter system, dubbed BUSSARD, was designed and implemented.