7,263 research outputs found

    Addressing the Multi-Channel Inverse Problem at High Energy Colliders: A Model Independent Approach to the Search for New Physics with Trileptons

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    We describe a method for interpreting trilepton searches at high energy colliders in a model-independent fashion and apply it to the recent searches at the Tevatron. The key step is to recognize that the trilepton signature is comprised of four experimentally very different channels defined by the number of tau-leptons in the trilepton state. Contributions from these multiple channels to the overall experimental sensitivity (cross section times branching ratio) are model-independent and can be parametrized in terms of relevant new particle masses. Given the trileptonic branching ratios of a specific model, these experimentally obtained multichannel sensitivities can be combined to obtain a cross section measurement that can be used to confront the model with data. Our model-independent results are more widely applicable than the current Tevatron trilepton results which are stated exclusively in terms of mSUGRA parameters of supersymmetry. The technique presented here can be expanded beyond trilepton searches to the more general "inverse problem" of experimentally discriminating between competing models that seek to explain new physics discovered in multiple channels.Comment: 17 pages, 7 figures Changed content cosmetic changes for submission to JHE

    Roller Testing to Mimic Damage of the ISS SARJ Ring and Durability Test to Simulate Fifteen Years of SARJ Operation Using the Damaged Surface

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    The International Space Station's starboard Solar Alpha Rotary Joint (SARJ) experienced a breakdown of the joint's race ring surface. The starboard SARJ mechanism was cleaned and lubricated with grease. To provide some guidance on the expected behavior of the damaged SARJ ring with continued operations, experiments were conducted using rollers and a vacuum roller test rig. The approach of the experimental work involved three main steps: (1) initiate damage using conditions representative of the SARJ with inadequate lubrication; (2) propagate the damage by operating the test rollers without lubrication; and (3) assess the durability of the roller by testing to simulate the equivalent of 15 years of SARJ operation on the damaged surface assuming adequate grease lubrication. During the rig testing, additional and/or replacement grease was introduced at regular intervals to maintain good lubrication in the rig. The damage to the nitride layer continued even after application of grease. The grease lubrication proved to be effective for limiting the value of the axial force that can be developed. Limiting the axial force on the SARJ mechanism is important since the larger the axial force the more concentrated the load pressure becomes on the blend-radius location on the SARJ roller. After the testing simulating 15 years of SARJ operations, the wear depths were the order of 0.2 mm for the nitrided 15-5 roller and the order of 0.06 mm for the mating 440C roller. Metallographic inspections were done to search for indications of impending fatigue or other fracture indications that might eventually propagate and cause structural failure. There were no indications or features found that could eventually compromise structural integrity

    Structure of FcRY, an avian immunoglobulin receptor related to mammalian mannose receptors, and its complex with IgY

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    Fc receptors transport maternal antibodies across epithelial cell barriers to passively immunize newborns. FcRY, the functional counterpart of mammalian FcRn (a major histocompatibility complex homolog), transfers IgY across the avian yolk sac, and represents a new class of Fc receptor related to the mammalian mannose receptor family. FcRY and FcRn bind immunoglobulins at pH ≤6.5, but not pH ≥7, allowing receptor–ligand association inside intracellular vesicles and release at the pH of blood. We obtained structures of monomeric and dimeric FcRY and an FcRY–IgY complex and explored FcRY's pH-dependent binding mechanism using electron cryomicroscopy (cryoEM) and small-angle X-ray scattering. The cryoEM structure of FcRY at pH 6 revealed a compact double-ring “head,” in which the N-terminal cysteine-rich and fibronectin II domains were folded back to contact C-type lectin-like domains 1–6, and a “tail” comprising C-type lectin-like domains 7–8. Conformational changes at pH 8 created a more elongated structure that cannot bind IgY. CryoEM reconstruction of FcRY dimers at pH 6 and small-angle X-ray scattering analysis at both pH values confirmed both structures. The cryoEM structure of the FcRY–IgY revealed symmetric binding of two FcRY heads to the dimeric FcY, each head contacting the CH4 domain of one FcY chain. FcRY shares structural properties with mannose receptor family members, including a head and tail domain organization, multimerization that may regulate ligand binding, and pH-dependent conformational changes. Our results facilitate understanding of immune recognition by the structurally related mannose receptor family and comparison of diverse methods of Ig transport across evolution
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