111 research outputs found

    Jet-Tagged Back-Scattering Photons For Quark Gluon Plasma Tomography

    Full text link
    Several sources of direct photons are known to contribute to the total photon yield in high energy nuclear collisions. All of these photons carry characteristic and important information on the initial nuclei or the hot and dense fireball created in the collision. We investigate the possibility to separate photons from back-scattering of high momentum quarks off quark gluon plasma from other sources. Their unique kinematics can be utilized through high energy jet triggers on the away-side. We discuss the basic idea and estimate the feasibility of such a measurement at RHIC and LHC.Comment: Contribution to Hard Probes 2012; 4 pages, 4 figure

    The structure of NMB1585, a MarR-family regulator from Neisseria meningitidis

    Get PDF
    The structure of the MarR-family regulator NMB1585 from N. meningitidis has been solved using data extending to 2.1 Å resolution

    Crystal structure of nitrogen regulatory protein IIA(Ntr )from Neisseria meningitidis

    Get PDF
    BACKGROUND: The NMB0736 gene of Neisseria meningitidis serogroup B strain MC58 encodes the putative nitrogen regulatory protein, IIA(Ntr )(abbreviated to NM-IIA(Ntr)). The homologous protein present in Escherichia coli is implicated in the control of nitrogen assimilation. As part of a structural proteomics approach to the study of pathogenic Neisseria spp., we have selected this protein for structure determination by X-ray crystallography. RESULTS: The NM-IIA(Ntr )was over-expressed in E. coli and was shown to be partially mono-phosphorylated, as assessed by mass spectrometry of the purified protein. Crystals of un-phosphorylated protein were obtained and diffraction data collected to 2.5 Å resolution. The structure of NM-IIA(Ntr )was solved by molecular replacement using the coordinates of the E. coli nitrogen regulatory protein IIA(ntr )[PDB: 1A6J] as the starting model. The overall fold of the Neisseria enzyme shows a high degree of similarity to the IIA(Ntr )from E. coli, and the position of the phosphoryl acceptor histidine residue (H67) is conserved. The orientation of an adjacent arginine residue (R69) suggests that it may also be involved in coordinating the phosphate group. Comparison of the structure with that of E. coli IIA(mtl )complexed with HPr [PDB: 1J6T] indicates that NM-IIA(Ntr )binds in a similar way to the HPr-like enzyme in Neisseria. CONCLUSION: The structure of NM-IIA(Ntr )confirms its assignment as a homologue of the IIA(Ntr )proteins found in a range of other Gram-negative bacteria. We conclude that the NM- IIA(Ntr )protein functions as part of a phosphorylation cascade which, in contrast to E. coli, shares the upstream phosphotransfer protein with the sugar uptake phosphoenolpyruvate:sugar phosphotransferase system (PTS), but in common with E. coli has a distinct downstream effector mechanism

    Measurement of the Isolated Photon Cross Section in p-pbar Collisions at sqrt{s}=1.96 TeV

    Get PDF
    The cross section for the inclusive production of isolated photons has been measured in p anti-p collisions at sqrt{s}=1.96 TeV with the D0 detector at the Fermilab Tevatron Collider. The photons span transverse momenta 23 to 300 GeV and have pseudorapidity |eta|<0.9. The cross section is compared with the results from two next-to-leading order perturbative QCD calculations. The theoretical predictions agree with the measurement within uncertainties.Comment: 7 pages, 5 figures, submitted to Phys.Lett.
    corecore