A Scintillating-fiber Beam Profile Monitor for the DAFNE BTF
A scintillating-fiber beam profile detector has been designed, built and tested, for the monitoring of the position and size of the electron beam of the DAFNE, the recently commissioned electron beam-test facility at the Frascati LNF. A description of the detector construction and assembly, together with the results achieved during the 2003-2004 run, are here reported.
Performance and upgrade of the DAFNE Beam Test Facility (BTF)
The DAFNE Beam Test Facility (BTF) at the Frascati National Laboratory of INFN (LNF) has been operational since October 2002. This facility provides electron and positron beams with tunable energy from 25 MeV to 750 MeV, while the intensity can be varied from 10/sup 10//pulse @ 0-50 Hz down to a single particle. In the last two years many experiments and beam tests have been hosted, so that the large use of the facility pushed the DAFNE staff to upgrade both the beam line, in order to improve the duty cycle, limited by frequent beam injection in the DAFNE main rings, and the diagnostic devices. The beam characteristics, the user experience and their typical measurements, the diagnostic tools developed and the available equipment are presented. Finally, we report on the facility upgrade and on operation in the new configuration.
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.