We report the WIMP dark matter search results using the first physics-run data of the PandaX-II 500 kg liquid xenon dual-phase time-projection chamber, operating at the China JinPing underground Laboratory. No dark matter candidate is identified above background. In combination with the data set during the commissioning run, with a total exposure of 3.3×10 4 kg-day, the most stringent limit to the spin-independent interaction between the ordinary and WIMP dark matter is set for a range of dark matter mass between 5 and 1000 GeV/c 2 . The best upper limit on the scattering cross section is found 2.5 × 10 −46 cm 2 for the WIMP mass 40 GeV/c 2 at 90% confidence level.Weakly interacting massive particles, WIMPs in short, are a class of hypothetical particles that came into existence shortly after the Big Bang. The WIMPs could naturally explain the astronomical and cosmological evidences of dark matter in the Universe. The weak interactions between WIMPs and ordinary matter could lead to the recoils of atomic nuclei that produce detectable signals in deep-underground direct detection experiments. Over the past decade, the dual-phase xenon time-projection chambers (TPC) emerged as a powerful technology for WIMP searches both in scaling up the target mass, as well as in improving background rejection [1][2][3]. LUX, a dark matter search experiment with a 250 kg liquid xenon target, has recently reported the best limit of 6×10 −46 cm 2 on the WIMP-nucleon scattering cross section [4] The PandaX-II experiment, a half-ton scale dual-phase xenon experiment at the China JinPing underground Laboratory (CJPL), has recently reported the dark matter search results from its commissioning run (Run 8,19.1 live days) with a 5845 kg-day exposure [5]. The data were contaminated with significant 85 Kr background. After a krypton distillation campaign in early 2016, PandaX-II commenced physics data taking in March 2016. In this paper, we report the combined WIMP search results using the data from the first physics run from March 9 to June 30, 2016 (Run 9, 79.6 live days) and Run 8, with a total of 3.3×10 4 kg-day exposure, the largest reported WIMP data set among dual-phase xenon detectors in the world to date.The PandaX-II detector has been described in detail in Ref. [5]. The liquid xenon target consists of a cylindrical TPC with dodecagonal cross section (opposite-side distance 646 mm), confined by the polytetrafluoroethylene (PTFE) reflective wall, and a vertical drift distance of 600 mm defined by the cathode mesh and gate grid located at the bottom and top. For each physical event, the prompt scintillation photons (S1) and the delayed electroluminescence photons (S2) from the ionized electrons are collected by two arrays of 55 Hamamatsu R11410-arXiv:1607.07400v3 [hep-ex] Hamamatsu R8520-406 1-inch PMTs serving as an active veto. The γ background, which produces electron recoil (ER) events, can be distinguished from the dark matter nuclear recoil (NR) using the S2-to-S1 ratio. During the data taking period in Run 9, a few diffe...

We have determined the crystal structure of the proteolytic component of the caseinolytic Clp protease (ClpP) from E. coli at 2.3 A resolution using an ab initio phasing procedure that exploits the internal 14-fold symmetry of the oligomer. The structure of a ClpP monomer has a distinct fold that defines a fifth structural family of serine proteases but a conserved catalytic apparatus. The active protease resembles a hollow, solid-walled cylinder composed of two 7-fold symmetric rings stacked back-to-back. Its 14 proteolytic active sites are located within a central, roughly spherical chamber approximately 51 A in diameter. Access to the proteolytic chamber is controlled by two axial pores, each having a minimum diameter of approximately 10 A. From the structural features of ClpP, we suggest a model for its action in degrading proteins.

The discovery of the RNA self-splicing group I intron provided the first demonstration that not all enzymes are proteins. Here we report the X-ray crystal structure (3.1-A resolution) of a complete group I bacterial intron in complex with both the 5'- and the 3'-exons. This complex corresponds to the splicing intermediate before the exon ligation step. It reveals how the intron uses structurally unprecedented RNA motifs to select the 5'- and 3'-splice sites. The 5'-exon's 3'-OH is positioned for inline nucleophilic attack on the conformationally constrained scissile phosphate at the intron-3'-exon junction. Six phosphates from three disparate RNA strands converge to coordinate two metal ions that are asymmetrically positioned on opposing sides of the reactive phosphate. This structure represents the first splicing complex to include a complete intron, both exons and an organized active site occupied with metal ions.

The second messenger signaling molecule bis-(3′-5′)-cyclic dimeric guanosine monophosphate (c-di-GMP) regulates many processes in bacteria, including motility, pathogenesis, and biofilm formation. c-di-GMP–binding riboswitches are important downstream targets in this signaling pathway. Here we report the crystal structure, at 2.7 Å resolution, of a c-di-GMP riboswitch aptamer from Vibrio cholerae bound to c-di-GMP, showing that the ligand binds within a three-helix junction that involves base-pairing and extensive base-stacking. The symmetric c-di-GMP is recognized asymmetrically with respect to both the bases and the backbone. A mutant aptamer was engineered that preferentially binds the candidate signaling molecule c-di-AMP over c-di-GMP. Kinetic and structural data suggest that genetic regulation by the c-di-GMP riboswitch is kinetically controlled and that gene expression is modulated through the stabilization of a previously unidentified P1 helix, illustrating a direct mechanism for c-di-GMP signaling.

Isoleucyl-transfer RNA (tRNA) synthetase (IleRS) joins Ile to tRNA(Ile) at its synthetic active site and hydrolyzes incorrectly acylated amino acids at its editing active site. The 2.2 angstrom resolution crystal structure of Staphylococcus aureus IleRS complexed with tRNA(Ile) and Mupirocin shows the acceptor strand of the tRNA(Ile) in the continuously stacked, A-form conformation with the 3' terminal nucleotide in the editing active site. To position the 3' terminus in the synthetic active site, the acceptor strand must adopt the hairpinned conformation seen in tRNA(Gln) complexed with its synthetase. The amino acid editing activity of the IleRS may result from the incorrect products shuttling between the synthetic and editing active sites, which is reminiscent of the editing mechanism of DNA polymerases.