During runaway discharges in TEXTOR, intense infrared (IR) radiation is-emitted in the electron flow direction. This can only be explained by synchrotron radiation of fast electrons. The observed spectral dependence is consistent with electrons of 25-30 MeV energy; the intensity corresponds to about 1016 electrons or to an electrical current of 40 kA. From the spatial structure of the observed IR pattern, new insight into the spatial distribution of the runaway electrons and their perpendicular momentum can be gained. The runaway electrons populate a torus with a diameter of 0.5-0.6 m, which is slightly larger than the plasma radius; the perpendicular momentum is determined from the vertical extent of the IR pattern and amounts to about 5 m0c. The transformation rate of electrons to runaways can be estimated from the time delay of the IR signal as 2 × 10−4 s−1; this agrees with theoretical expectations derived from the ratio of the electrical field strength to the critical field strength. In TEXTOR, runaways are confined up to energies of 50 MeV, which is just below the limit where a phase should exist in which runaways radiate as much energy as they gain per turn.

perturbation approach, we seek modeling errors in the The ever-increasing demand for better performance from following parameters circular accelerators requires improved methods to calibrate • Quadrupole gradients the optics model. We present a linear perturbation approach to°Corrector scale factors the calibration problem in which the modeled BPM-to-• BPM scale factors corrector response matrix is expanded to first order in • BPM resolution errors .,:,:a_rupole strengths. The result is numerically fit to the measured response matrix yielding quadrupole strength errors, including a comprehensive error analysis of the results. From corrector strength errors, and BPM linearity factors. The large the difference orbit measurements, we first determine the number of degrees of freedom in the fit allows a BPM-to-correctorresponsenmtrixcoefficients comprehensive error analysis, including the determination of Ax at BPM i BPM resolutions. In this way, a self-consistent first order _ij = (1) optics model of SPEAR was generated which reproduces the Ax' at corrector j measured tunes, which are then compared to the perturbed expression for the

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PLC(Bc) is a 28.5 kDa monomeric enzyme that catalyzes the hydrolysis of the phosphodiester bond of phosphatidylcholine, phosphatidylethanolamine, and phosphatidylserine to provide a diacylglycerol and the corresponding phosphorylated headgroup. Because single replacements of Glu4, Tyr56, and Phe66 in the headgroup binding pocket led to changes in substrate specificity [Martin et al. (2000) Biochemistry 39, 3410-3415], a combinatorial library of approximately 6000 maltose binding protein-PLC(Bc) fusion protein mutants containing random permutations of these three residues was generated to identify PLC(Bc) mutants with altered specificity profiles and high catalytic activities. Members of this library were screened for hydrolytic activity toward the water soluble substrates C6PC, C6PE, and C6PS using a novel protocol that was conducted in a 96-well format and featured the in situ cleavage of the fusion protein to release the mutant PLC(Bc)s. Ten mutant enzymes that exhibited significant preferences toward C6PE or C6PS were selected and analyzed by steady-state kinetics to determine their specificity constants, k(cat)/K(M). The C6PS selective clones E4G, E4Q/Y56T/F66Y, and E4K/Y56V exhibited higher specificity constants toward C6PS than wt, whereas Y56T, F66Y, and Y56T/F66Y were C6PE selective and had comparable or higher specificity constants than wt for C6PE. The corresponding wt residues were singly reinserted back into the E4Q/Y56T/F66Y and E4K/Y56V mutants via site-directed mutagenesis, and the E4Q/F66Y mutant thus obtained exhibited a 10-fold higher specificity constant toward C6PS than wt, a value significantly higher than other PLC(Bc) mutants. On the basis of available data, an aromatic residue at position 66 appears important for significant catalytic activity toward all three substrates, especially C6PC and C6PE. The charge of residue 4 also appears to be a determinant of enzyme specificity as a negatively charged residue at this position endows the enzyme with C6PC and C6PE preference, whereas a polar neutral or positively charged residue results in C6PS selectivity. Replacing Tyr56 with Val, Ala, Thr, or Ser greatly reduces activity toward C6PC. Thus, the substrate specificity of PLC(Bc) can be modulated by varying three of the amino acid residues that constitute the headgroup binding pocket, and it is now apparent that this enzyme is not evolutionarily optimized to hydrolyze phospholipids with ethanolamine or serine headgroups.

Four new low field side antennae grouped in pairs have been installed on TEXTOR. It is found that the interaction with the wall (density rise, impurity generation) is significantly reduced when operating each pair out of phase (E) as opposed to in phase (0). The beneficial effect in the n configuration is obtained without drop in plasma loading. This experimental property is shown, from theory, to be explained by the judicious choice of the geometrical configuration. A further improvement in the wall interaction is made possible by an appropriate choice of wall conditioning (wall carbonization with liner at 400'C or. above all, boronization). As a result record low values of PYsd/Ptota, were achieved during ICRH. The large reduction in wall interaction during ICRH allows routine long pulse (> 1 s) ICRH operation at the maximum power level available (g 2.5 MW).