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The island divertor concept has successfully been realized at W7-AS. The divertor gives access to a new NBI-heated high density regime with densities up to 4×10²⁰m-3 and energy confinement well above customary scalings. This regime appears promising with respect to the requirements of both confinement and exhaust. Many features are reminiscent of a quiescent H-mode, but plasma particle transport behaves differently. Beyond a threshold density energy confinement approximately doubles whereas particle confinement dramatically decreases. The density profile flattens and the inward impurity pinch is reduced. This eases density control, prevents impurity accumulation, and allows for quasi-stationary conditions with radiation profiles peaked at the edge. At the highest densities partial detachment occurs with a radiated power fraction up to 90% at a tolerable expense of plasma energy. The sub-divertor pressure is sufficient for pumping. Major experimental results, such as the lack of a high recycling phase preceding detachment, are also predicted by the EMC3/EIRENE code.

W7-AS operates with an island divertor, which utilises the natural edge islands of the low-shear stellarator configuration to divert the plasma. High densities (up to 4×1020m-3) and partly detached divertor conditions have been attained. The details of the divertor operation will be described along with the 3D-efforts to model the divertor observations. At a density beyond 1.5×1020m-3 another confinement bifurcation appears, which allows steady state operation at good energy and low impurity confinement. The transition is possible from a state of normal confinement or from ELMy or quiescent H-modes. Starting with normal confinement, bifurcation is initiated by a broadening of the density profile. This regime can easily be heated above cut-off by ECRH using electron-bernstein-wave mode conversion. The highest beta-values (>3%) are achieved at high density. The relevance of the W7-AS data for Wendelstein 7-X and the Helias-reactor will be discussed.

Investigations of the performance and stability of high-beta plasmas have been restarted in W7-AS utilizing higher heating powers and the new divertor system. The combination of beneficial effects resulted in a significant increase of the volume averaged β from 2 % up to 3.1 % and in MHD-quiescent, quasi-stationary discharges at low radiation levels. Experimental studies of equilibrium effects and of MHD mode activity have been performed with the X-ray tomography system. In addition results of computational MHD stability studies are presented, which show an increase of the stability with increasing β due to the pressure induced deepening of the magnetic well in combination with increasing magnetic shear, in qualitative agreement with the experimental data. The maximum achieved β is limited by the available heating power and not by stability effects. The equilibrium β-limit is approached in the case of low-iota configurations. Particularly with regard to current carrying stellarators and comparisons with tokamaks the modification of the stability of high-beta plasmas by significant OH-currents has been investigated.

L(+)-lactate dehydrogenase (LDH; E.C.1.1.1.27) from the hyperthermophilic bacterium Thermotoga maritima has been shown to represent the most stable LDH isolated so far (Wrba A, Jaenicke R, Huber R, Stetter KO, 1990, Eur J Biochem 188:195-201). In order to obtain the enzyme in amounts sufficient for physical characterization, and to analyze the molecular basis of its intrinsic stability, the gene was cloned and expressed functionally in Escherichia coli. Growth of the cells and purification of the enzyme were performed aerobically at 26 degrees C, i.e., ca. 60 degrees below the optimal growth temperature of Thermotoga. Two enzyme species with LDH activity were purified to homogeneity. Crystals of the enzyme obtained at 4 degrees C show satisfactory diffraction suitable for X-ray analysis up to a resolution of 2.8 A. As shown by gel-permeation chromatography, chemical crosslinking, light scattering, analytical ultracentrifugation, and electron microscopy, the two LDH species represent homotetramers and homooctamers (i.e., dimers of tetramers), with a common subunit molecular mass of 35 kDa. The spectroscopic characteristics (UV absorption, fluorescence emission, near- and far-UV CD) of the two species are indistinguishable. The calculated alpha-helix content is 45%, in accordance with the result of homology modeling. Compared to the tetrameric enzyme, the octamer exhibits reduced specific activity, whereas KM is unalatered. The extreme intrinsic stability of the protein is reflected by its unaltered catalytic activity over 4 h at 85 degrees C; irreversible thermal denaturation becomes significant at approximately 95 degrees C. The anomalous resistance toward chemical denaturation using guanidinium chloride and urea confirms this observation. Both the high optimal temperature and the pH optimum of the catalytic activity correspond to the growth conditions of T. maritima in its natural habitat.

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An important question in protein folding is whether compact substructures or domains are autonomous units of folding and assembly. The protomer of the tetrameric D-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima has a complex coenzyme-binding domain, in which residues 1-146 form a compact substructure with the last 31 residues (313-333). Here it is shown that the gene of a single-chain protein can be expressed in Escherichia coli after deleting the 163 codons corresponding to the interspersed catalytic domain (150-312). The purified gene product is a soluble, monomeric protein that binds both NAD+ and NADH strongly and possesses the same unfolding transition induced by guanidinium chloride as the native tetramer. The autonomous folding of the coenzyme-binding domain has interesting implications for the folding, assembly, function, and evolution of the native enzyme.

D-Lactate dehydrogenase from the extreme halophilic archaebacterium Halobacterium marismortui has been partially purified by ammonium-sulfate fractionation, hydrophobic and ion exchange chromatography. Catalytic activity of the enzyme requires salt concentrations beyond 1M NaCl: optimum conditions are 4M NaCl or KCl, pH 6-8, 50 degrees C. Michaelis constants for NADH and pyruvate under optimum conditions of enzymatic activity are 0.070 and 4.5mM, respectively. As for other bacterial D-specific lactate dehydrogenases, fructose 1,6-bisphosphate and divalent cations (Mg2+, Mn2+) do not affect the catalytic activity of the enzyme. As shown by gel-filtration and ultracentrifugal analysis, the enzyme under the conditions of the enzyme assay is a dimer with a subunit molecular mass close to 36 kDa. At low salt concentrations (less than 1M), as well as high concentrations of chaotropic solvent components and low pH, the enzyme undergoes reversible deactivation, dissociation and denaturation. The temperature dependence of the enzymatic activity shows non-linear Arrhenius behavior with activation energies of the order of 90 and 25 kJ/mol at temperatures below and beyond ca. 30 degrees C. In the presence of high salt, the enzyme exhibits exceptional thermal stability; denaturation only occurs at temperatures beyond 55 degrees C. The half-time of deactivation at 70 and 75 degrees C is 300 and 15 min, respectively. Maximum stability is observed at pH 7.5-9.0.