234 research outputs found

    Phase-sensitive detection of Bragg scattering at 1D optical lattices

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    We report on the observation of Bragg scattering at 1D atomic lattices. Cold atoms are confined by optical dipole forces at the antinodes of a standing wave generated by the two counter-propagating modes of a laser-driven high-finesse ring cavity. By heterodyning the Bragg-scattered light with a reference beam, we obtain detailed information on phase shifts imparted by the Bragg scattering process. Being deep in the Lamb-Dicke regime, the scattered light is not broadened by the motion of individual atoms. In contrast, we have detected signatures of global translatory motion of the atomic grating.Comment: 4 pages, 4 figure

    Quantum-degenerate mixture of fermionic lithium and bosonic rubidium gases

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    We report on the observation of sympathetic cooling of a cloud of fermionic 6-Li atoms which are thermally coupled to evaporatively cooled bosonic 87-Rb. Using this technique we obtain a mixture of quantum-degenerate gases, where the Rb cloud is colder than the critical temperature for Bose-Einstein condensation and the Li cloud colder than the Fermi temperature. From measurements of the thermalization velocity we estimate the interspecies s-wave triplet scattering length |a_s|=20_{-6}^{+9} a_B. We found that the presence of residual rubidium atoms in the |2,1> and the |1,-1> Zeeman substates gives rise to important losses due to inelastic collisions.Comment: 4 pages, 3 figure

    Highly versatile atomic micro traps generated by multifrequency magnetic field modulation

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    We propose the realization of custom-designed adiabatic potentials for cold atoms based on multimode radio frequency radiation in combination with static inhomogeneous magnetic fields. For example, the use of radio frequency combs gives rise to periodic potentials acting as gratings for cold atoms. In strong magnetic field gradients the lattice constant can be well below 1 micrometer. By changing the frequencies of the comb in time the gratings can easily be propagated in space, which may prove useful for Bragg scattering atomic matter waves. Furthermore, almost arbitrarily shaped potential are possible such as disordered potentials on a scale of several 100 nm or lattices with a spatially varying lattice constant. The potentials can be made state selective and, in the case of atomic mixtures, also species selective. This opens new perspectives for generating tailored quantum systems based on ultra cold single atoms or degenerate atomic and molecular quantum gases.Comment: 12 pages, 6 figure

    [Evaluation of malaria rapid diagnostic test Optimal-IT® pLDH along the Plasmodium falciparum distribution limit in Mauritania].

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    Performance of the malaria Rapid Diagnostic Test (RDT) OptiMal-IT® was evaluated in Mauritania where malaria is low and dependent on a short transmission season. Slide microscopy was considered as the reference method of diagnosis. Febrile patients with suspected malaria were recruited from six health facilities, 3 urban and 3 rural, during two periods (December 2011 to February 2012, and August 2012 to March 2013). Overall, 780 patients were sampled, with RDT and thick blood film microscopy results being obtained for 759 of them. Out of 774 slides examined, of which 200 were positive, P. falciparum and P. vivax mono-infections were detected in 63.5% (127) and 29.5% (59), while P. falciparum/P. vivax coinfections were detected in 7% (14). Both species were observed in all study sites, although in significantly different proportions. The proportions of thick blood film and OptiMal-IT® RDT positive individuals was 26.3% and 30.3% respectively. Sensitivity and specificity of OptiMal-IT® RDT were 89% [95% CI, 84.7-93.3] and 91.1% [88.6-93.4]. Positives and negative predictive values were 78.1% [72.2-83.7] and 95.9% [94.1-97.5]. These diagnostic values are similar to those generally reported elsewhere, and support the use of RDTs as the main diagnostic tool for malaria in Mauritanian health facilities. In the future, choice of RDTs to be used must take account of thermostability in a hot, dry environment and their ability to detect P. falciparum and P. vivax

    Autogenous regulation of Escherichia coli polynucleotide phosphorylase expression revisited

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    The Escherichia coli polynucleotide phosphorylase (PNPase, encoded by pnp), a phosphorolytic exoribonuclease, post-transcriptionally regulates its own expression at the level of mRNA stability and translation. Its primary transcript is very efficiently processed by RNase III, an endonuclease that makes a staggered double strand cleavage about in the middle of a long stem-loop in the 5'-untranslated region. The processed pnp mRNA is then rapidly degraded in a PNPase-dependent manner. Two non-mutually exclusive models have been proposed to explain PNPase autogenous regulation. The earlier one suggested that PNPase impedes translation of the RNase III processed pnp mRNA thus exposing the transcript to degradative pathways. More recently this has been replaced by the current model, which maintains that PNPase would simply degrade the promoter proximal small RNA generated by the RNase III endonucleolytic cleavage thus destroying the double stranded structure at the 5'-end that otherwise stabilizes the pnp mRNA. In our opinion, however, the first model was not completely ruled out. Moreover, the RNA decay pathway acting upon the pnp mRNA after disruption of the 5' double stranded structure remained to be determined. Here we provide additional support to the current model and show that the RNase III-processed pnp mRNA devoid of the double stranded structure at its 5'-end is not translatable and is degraded by RNase E in a PNPase-independent manner. Thus the role of PNPase in autoregulation is simply to remove, in concert with RNase III, the 5'-fragment of the cleaved structure that both allows translation and prevents the RNase E-mediated PNPase-independent degradation of the pnp transcript

    BCS and BEC p-wave pairing in Bose-Fermi gases

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    The pairing of fermionic atoms in a mixture of atomic fermion and boson gases at zero temperature is investigated. The attractive interaction between fermions, that can be induced by density fluctuations of the bosonic background, can give rise to a superfluid phase in the Fermi component of the mixture. The atoms of both species are assumed to be in only one internal state, so that the pairing of fermions is effective only in odd-l channels. No assumption about the value of the ratio between the Fermi velocity and the sound velocity in the Bose gas is made in the derivation of the energy gap equation. The gap equation is solved without any particular "ansatz" for the pairing field or the effective interaction. The p-wave superfluidity is studied in detail. By increasing the strength and/or decreasing the range of the effective interaction a transition of the fermion pairing regime, from the Bardeen-Cooper-Schrieffer state to a system of tightly bound couples can be realized. These composite bosons behave as a weakly-interacting Bose-Einstein condensate.Comment: 14 pages, 6 eps-figures. To be published in European Physical Journal

    Dissecting Escherichia coli outer membrane biogenesis using differential proteomics

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    The cell envelope of Gram-negative bacteria is a complex multi-layered structure comprising an inner cytoplasmic membrane and an additional asymmetric lipid bilayer, the outer membrane, which functions as a selective permeability barrier and is essential for viability. Lipopolysaccharide, an essential glycolipid located in the outer leaflet of the outer membrane, greatly contributes to the peculiar properties exhibited by the outer membrane. This complex molecule is transported to the cell surface by a molecular machine composed of seven essential proteins LptABCDEFG that form a transenvelope complex and function as a single device. While advances in understanding the mechanisms that govern the biogenesis of the cell envelope have been recently made, only few studies are available on how bacterial cells respond to severe envelope biogenesis defects on a global scale. Here we report the use of differential proteomics based on Multidimensional Protein Identification Technology (MudPIT) to investigate how Escherichia coli cells respond to a block of lipopolysaccharide transport to the outer membrane. We analysed the envelope proteome of a lptC conditional mutant grown under permissive and non permissive conditions and identified 123 proteins whose level is modulated upon LptC depletion. Most such proteins belong to pathways implicated in cell envelope biogenesis, peptidoglycan remodelling, cell division and protein folding. Overall these data contribute to our understanding on how E. coli cells respond to LPS transport defects to restore outer membrane functionality. \ua9 2014 Martorana et al

    The Escherichia coli Lpt transenvelope protein complex for lipopolysaccharide export is assembled via conserved structurally homologous domains

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    Lipopolysaccharide is a major glycolipid component in the outer leaflet of the outer membrane (OM), a peculiar permeability barrier of Gram-negative bacteria that prevents many toxic compounds from entering the cell. Lipopolysaccharide transport (Lpt) across the periplasmic space and its assembly at the Escherichia coli cell surface are carried out by a transenvelope complex of seven essential Lpt proteins spanning the inner membrane (LptBCFG), the periplasm (LptA), and the OM (LptDE), which appears to operate as a unique machinery. LptC is an essential inner membrane-anchored protein with a large periplasm-protruding domain. LptC binds the inner membrane LptBFG ABC transporter and interacts with the periplasmic protein LptA. However, its role in lipopolysaccharide transport is unclear. Here we show that LptC lacking the transmembrane region is viable and can bind the LptBFG inner membrane complex; thus, the essential LptC functions are located in the periplasmic domain. In addition, we characterize two previously described inactive single mutations at two conserved glycines (G56V and G153R, respectively) of the LptC periplasmic domain, showing that neither mutant is able to assemble the transenvelope machinery. However, while LptCG56V failed to copurify any Lpt component, LptCG153R was able to interact with the inner membrane protein complex LptBFG. Overall, our data further support the model whereby the bridge connecting the inner and outer membranes would be based on the conserved structurally homologous jellyroll domain shared by five out of the seven Lpt components
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