Lab Directorate
ALS-U (36)
Irradiation of materials with short, intense ion pulses at NDCX-II
We present an overview of the performance of the Neutralized Drift Compression Experiment-II (NDCX-II) accelerator at Berkeley Lab, and report on recent target experiments on beam-driven melting and transmission ion energy loss measurements with nanosecond and millimeter-scale ion beam pulses and thin tin foils. Bunches with around 1011 ions, 1 mm radius, and 2-30 ns full width at half maximum duration have been created with corresponding fluences in the range of 0.1-0.7 J/cm2. To achieve these short pulse durations and mm-scale focal spot radii, the 1.1 MeV [megaelectronvolt (106 eV)] He+ ion beam is neutralized in a drift compression section, which removes the space charge defocusing effect during final compression and focusing. The beam space charge and drift compression techniques resemble necessary beam conditions and manipulations in heavy ion inertial fusion accelerators. Quantitative comparison of detailed particle-in-cell simulations with the experiment plays an important role in optimizing accelerator performance.
Source-to-accelerator quadrupole matching section for a compact linear accelerator
Recently, we presented a new approach for a compact radio-frequency (RF) accelerator structure and demonstrated the functionality of the individual components: acceleration units and focusing elements. In this paper, we combine these units to form a working accelerator structure: a matching section between the ion source extraction grids and the RF-acceleration unit and electrostatic focusing quadrupoles between successive acceleration units. The matching section consists of six electrostatic quadrupoles (ESQs) fabricated using 3D-printing techniques. The matching section enables us to capture more beam current and to match the beam envelope to conditions for stable transport in an acceleration lattice. We present data from an integrated accelerator consisting of the source, matching section, and an ESQ doublet sandwiched between two RF-acceleration units.
Projected WIMP sensitivity of the LUX-ZEPLIN dark matter experiment
LUX-ZEPLIN (LZ) is a next-generation dark matter direct detection experiment that will operate 4850 feet underground at the Sanford Underground Research Facility (SURF) in Lead, South Dakota, USA. Using a two-phase xenon detector with an active mass of 7 tonnes, LZ will search primarily for low-energy interactions with weakly interacting massive particles (WIMPs), which are hypothesized to make up the dark matter in our galactic halo. In this paper, the projected WIMP sensitivity of LZ is presented based on the latest background estimates and simulations of the detector. For a 1000 live day run using a 5.6-tonne fiducial mass, LZ is projected to exclude at 90% confidence level spin-independent WIMP-nucleon cross sections above 1.4×10-48 cm2 for a 40 GeV/c2 mass WIMP. Additionally, a 5σ discovery potential is projected, reaching cross sections below the exclusion limits of recent experiments. For spin-dependent WIMP-neutron(-proton) scattering, a sensitivity of 2.3×10-43 cm2 (7.1×10-42 cm2) for a 40 GeV/c2 mass WIMP is expected. With underground installation well underway, LZ is on track for commissioning at SURF in 2020.
Laboratory Directorate (321)
Identification and Characterization of the Major Porin of Desulfovibrio vulgaris Hildenborough
Due in large part to their ability to facilitate the diffusion of a diverse range of solutes across the outer membrane (OM) of Gram-negative bacteria, the porins represent one of the most prominent and important bacterial membrane protein superfamilies. Notably, for the Gram-negative bacterium Desulfovibrio vulgaris Hildenborough, a model organism for studies of sulfate-reducing bacteria, no genes for porins have been identified or proposed in its annotated genome. Results from initial biochemical studies suggested that the product of the DVU0799 gene, which is one of the most abundant proteins of the D. vulgaris Hildenborough OM and purified as a homotrimeric complex, was a strong porin candidate. To investigate this possibility, this protein was further characterized biochemically and biophysically. Structural analyses via electron microscopy of negatively stained protein identified trimeric particles with stain-filled depressions and structural modeling suggested a β-barrel structure for the monomer, motifs common among the known porins. Functional studies were performed in which crude OM preparations or purified DVU0799 was reconstituted into proteoliposomes and the proteoliposomes were examined for permeability against a series of test solutes. The results obtained establish DVU0799 to be a pore-forming protein with permeability properties similar to those observed for classical bacterial porins, such as those of Escherichia coli Taken together, these findings identify this highly abundant OM protein to be the major porin of D. vulgaris Hildenborough. Classification of DVU0799 in this model organism expands the database of functionally characterized porins and may also extend the range over which sequence analysis strategies can be used to identify porins in other bacterial genomes.IMPORTANCE Porins are membrane proteins that form transmembrane pores for the passive transport of small molecules across the outer membranes of Gram-negative bacteria. The present study identified and characterized the major porin of the model sulfate-reducing bacterium Desulfovibrio vulgaris Hildenborough, observing its preference for anionic sugars over neutral ones. Its predicted architecture appears to be novel for a classical porin, as its core β-barrel structure is of a type typically found in solute-specific channels. Broader use of the methods employed here, such as assays for channel permeability and electron microscopy of purified samples, is expected to help expand the database of confirmed porin sequences and improve the range over which sequence analysis-based strategies can be used to identify porins in other Gram-negative bacteria. Functional characterization of these critical gatekeeping proteins from divergent Desulfovibrio species should offer an improved understanding of the physiological features that determine their habitat range and supporting activities.
Production and Decay of Ξc0 at BABAR
Using 116.1 fb(-1) of data collected by the BABAR detector, we present an analysis of xi(c)(0) production in B decays and from the cc continuum, with the xi(c)(0) decaying into omega- K+ and xi- pi+ final states. We measure the ratio of branching fractions B(xi(c)(0) --> omega- K+)/B(xi(c)(0) --> xi- pi+) spectrum is measured on and 40 MeV below the upsilon(4S) resonance. From these spectra the branching fraction product B(B --> xi(c)(0)X) x B(xi(c)(0) --> xi- pi+) is measured to be (2.11 +/- 0.19 +/- 0.25) x 10(-4), and the cross-section product sigma(e+ e- --> xi(c)(0)X) x B(xi(c)(0) --> xi- pi+) from the continuum is measured to be (388 +/- 39 +/- 41) fb at a center-of-mass energy of 10.58 GeV.
Measurement of the average φ multiplicity in B meson decay
We present a measurement of the average multiplicity of φ mesons in [Formula Presented] [Formula Presented] and [Formula Presented] meson decays. Using 17.6 [Formula Presented] of data taken at the [Formula Presented] resonance by the BABAR detector at the PEP-II [Formula Presented] storage ring at the Stanford Linear Accelerator Center, we reconstruct φ mesons in the [Formula Presented] decay mode and measure [Formula Presented] This is significantly more precise than any previous measurement. © 2004 The American Physical Society.