Near-net-shape fabrication of continuous Ag-clad Bi-based superconductors
We have developed a near-net-shape process for Ag-clad Bi-2212 superconductors. This alternative to the powder-in-tube process offers the advantages of nearly continuous processing, minimization of processing steps, reasonable ability to control the Bi-2212/Ag ratio, and early development of favorable texture of the Bi-2212 grains. The powder is rolled into an Ag channel, a cap is applied, and the assembly is lightly rolled. To minimize distortion during heat treatment, it is especially important that the Bi-2212 powder be nearly free of volatile species such as carbon. A vacuum-calcination process was developed to control CO/sub 2/ evolution during heating. Superconducting properties are discussed.
Critical current in Tl-base high-Tc oxides synthesized through a diffusion process
In the TBCCO diffusion composites, the 2223 phase is easily formed within a short reaction time. The critical current at 77 K is significantly improved by the F addition to the coating layer. The F addition decreases the degradation of critical current under magnetic field at 77 K, and shifts the irreversibility line to higher temperature. The XRD study reveals that the F addition clearly promotes the phase transformation from 2223 to 1223. Meanwhile, the annealing in flowing O/sub 2/ at 550/spl deg/C-600/spl deg/C also increases the critical current at 71 K. A J/sub c/ of about 10,000 A/cm/sup 2/ is obtained at 77 K in the TBCCO diffusion layer by the F addition and the O/sub 2/ annealing.<<ETX>>
A single amino acid substitution in elongation factor Tu disrupts interaction between the ternary complex and the ribosome
Elongation factor Tu (EF-Tu).GTP has the primary function of promoting the efficient and correct interaction of aminoacyl-tRNA with the ribosome. Very little is known about the elements in EF-Tu involved in this interaction. We describe a mutant form of EF-Tu, isolated in Salmonella typhimurium, that causes a severe defect in the interaction of the ternary complex with the ribosome. The mutation causes the substitution of Val for Gly-280 in domain II of EF-Tu. The in vivo growth and translation phenotypes of strains harboring this mutation are indistinguishable from those of strains in which the same tuf gene is insertionally inactivated. Viable cells are not obtained when the other tuf gene is inactivated, showing that the mutant EF-Tu alone cannot support cell growth. We have confirmed, by partial protein sequencing, that the mutant EF-Tu is present in the cells. In vitro analysis of the natural mixture of wild-type and mutant EF-Tu allows us to identify the major defect of this mutant. Our data shows that the EF-Tu is homogeneous and competent with respect to guanine nucleotide binding and exchange, stimulation of nucleotide exchange by EF-Ts, and ternary complex formation with aminoacyl-tRNA. However various measures of translational efficiency show a significant reduction, which is associated with a defective interaction between the ribosome and the mutant EF-Tu.GTP.aminoacyl-tRNA complex. In addition, the antibiotic kirromycin, which blocks translation by binding EF-Tu on the ribosome, fails to do so with this mutant EF-Tu, although it does form a complex with EF-Tu. Our results suggest that this region of domain II in EF-Tu has an important function and influences the binding of the ternary complex to the codon-programmed ribosome during protein synthesis. Models involving either a direct or an indirect effect of the mutation are discussed.