Creation of NOON states by double Fock-state/Bose-Einstein condensates

NOON states (states of the form $|N>_{a}|0>_{b}+|0>_{a}|N>_{b}$ where $a$ and $b$ are single particle states) have been used for predicting violations of hidden-variable theories (Greenberger-Horne-Zeilinger violations) and are valuable in metrology for precision measurements of phase at the Heisenberg limit. We show theoretically how the use of two Fock state/Bose-Einstein condensates as sources in a modified Mach Zender interferometer can lead to the creation of the NOON state in which $a$ and $b$ refer to arms of the interferometer and $N$ is the total number of particles in the two condensates. The modification of the interferometer involves making conditional ``side'' measurements of a few particles near the sources. These measurements put the remaining particles in a superposition of two phase states, which are converted into NOON states by a beam splitter. The result is equivalent to the quantum experiment in which a large molecule passes through two slits. The NOON states are combined in a final beam splitter and show interference. Attempts to detect through which ``slit'' the condensates passed destroys the interference.Comment: 8 pages 5 figure

The glucosyl-l-phosphate transferase WchA (Cap8E) primes the capsular polysaccharide repeat unit biosynthesis of Spectrococcus pneumoniae serotype 8

International audienceThe gene wchA (cap8E) belongs to the cps8 locus that is involved in biosynthesis of the capsular polysaccharide (CPS) repeat unit (RU) of the virulent Streptococcus pneumoniae serotype 8. We report here the biochemical characterization of the membrane-associated protein WchA (Cap8E), overexpressed in Escherichia coli BL21(DE3)/pLysS. Our results demonstrate that the recombinant enzyme transfers in vitro a glucosyl-1-phosphate from UDP-glucose to an endogenous phosphoryl-polyprenol, thereby priming the RU biosynthetic pathway of S. pneumoniae CPS 8. We also show that the C-terminal half of WchA is the glycosyltransferase domain as observed for the galactosyl-1-phosphate transferase WbaP from Salmonella enterica, previously described to prime the first step of O-antigen biosynthesis. These results demonstrate that WchA plays a prominent function in the capsule biosynthesis and explain the key role it occupies in the pneumococcal capsule variation