Characteristics and outcomes of patients requiring rapid response system activation within 24 hours of emergency admission

Objectives:&nbsp;To establish the prevalence of emergency responses for clinical deterioration (cardiac arrest team or medical emergency team [MET] activation) within 24 hours of emergency admission, and determine if there were differences in characteristics and outcomes of ward patients whose emergency response was within, or beyond, 24 hours of emergency admission. Design, setting and participants: A retrospective, descriptive, exploratory study using MET, cardiac arrest, emergency department and inpatient databases, set in a 365-bed urban district hospital in Melbourne, Australia. Participants were adult hospital inpatients admitted to a medical or surgical ward via the emergency department (ED) who needed an emergency response for clinical deterioration during 2012. Main outcome measures: Inhospital mortality, unplanned intensive care unit admission and hospital length of stay (LOS). Results: A total of 819 patients needed an emergency response for clinical deterioration: 587 patients were admitted via the ED and 28.4% of emergency responses occurred within 24 hours of emergency admission. Patients whose first emergency response was within 24 hours of emergency admission (compared with beyond 24 hours) were more likely to be triaged to Australasian triage scale category 1 (5.4% v 1.2%, P=0.005), less likely to require ICU admission after the emergency response (7.6% v 13.9%, P=0.039), less likely to have recurrent emergency responses during their hospital stay (9.7% v 34%, P &lt; 0.001) and had a shorter median hospital LOS (7 days v 11 days, P &lt; 0.001). Conclusions: One-quarter of emergency responses after admission via the ED occurred within 24 hours. Further research is needed to understand the predictors of deterioration in patients needing emergency admission.</div

Measurement of the Lambda^0_b lifetime in the decay Lambda^0_b -> J/psi Lambda^0 with the D0 Detector

We present measurements of the Lambda^0_b lifetime in the exclusive decay channel Lambda^0_{b}->J/psi Lambda^0, with J/psi to mu+ mu- and Lambda^0 to p pi-, the B^0 lifetime in the decay B^0 -> J/psi K^0_S with J/psi to mu+ mu- and K^0_S to pi+ pi-, and the ratio of these lifetimes. The analysis is based on approximately 250 pb^{-1} of data recorded with the D0 detector in pp(bar) collisions at sqrt{s}=1.96 TeV. The Lambda^0_b lifetime is determined to be tau(Lambda^0_b) = 1.22 +0.22/-0.18 (stat) +/- 0.04 (syst) ps, the B^0 lifetime tau(B^0) = 1.40 +0.11/-0.10 (stat) +/- 0.03 (syst) ps, and the ratio tau(Lambda^0_b)/tau(B^0) = 0.87 +0.17/-0.14 (stat) +/- 0.03 (syst). In contrast with previous measurements using semileptonic decays, this is the first determination of the Lambda^0_b lifetime based on a fully reconstructed decay channel.Comment: 7 pages, 4 figures, Submitted to Physical Review Letters, v2: Added FNAL Pub-numbe

Erratum to Measurement of σ(ppˉ→Z)⋅Br(Z→ττ)\sigma (p \bar p \to Z) \cdot Br(Z \to \tau\tau) at s=\bm{\sqrt{s}=}1.96 TeV, published in Phys. Rev. D {71}, 072004 (2005)

A change in estimated integrated luminosity (from 226 pb$^{-1} to 257 pb$^{-1}$leads to a corrected value for${\sigma (p \bar p \to Z) \cdot}$Br${(Z \to \tau \tau)}$of$209\pm13(stat.)\pm16(syst.)\pm13(lum) pb

Measurement of the WW production cross section in p anti-p collisions at s**(1/2) = 1.96 TeV

We present a measurement of the W boson pair-production cross section in p anti-p collisions at a center-of-mass energy of sqrt{s}=1.96 TeV. The data, collected with the Run II DO detector, correspond to an integrated luminosity of 224-252 pb^-1 depending on the final state (ee, emu or mumu). We observe 25 candidates with a background expectation of 8.1+/-0.6(stat)+/-0.6(syst)+/-0.5(lum) events. The probability for an upward fluctuation of the background to produce the observed signal is 2.3x10^-7, equivalent to 5.2 standard deviations.The measurement yields a cross section of 13.8+4.3/-3.8(stat)+1.2/-0.9(syst)+/-0.9(lum) pb, in agreement with predictions from the standard model.Comment: submitted to PR

Crystallization of thermitase, a thermostable subtilisin, from a sodium formate solution by means of an automated procedure

A new crystal form of native thermitase has been obtained using sodium formate as the precipitating agent and employing an automated crystallization procedure. The crystals have the form of tetragonal bipyramids, the longest dimension being about 0.4 mm. The space group is and . The crystals diffract beyond 2.5

SOAKING IN CS2SO4 REVEALS A CAESIUM-AROMATIC INTERACTION IN -LIVER RHODANESE

Soaking crystals of rhodanese (thiosulphate:cyanide sulphurtransferase) in 2 M caesium sulphate reveals three caesium binding sites of this enzyme. One of these had been described before as a binding site for sodium ions and is located in a cleft close to the active site. In this site the monovalent cation is coordinated by five oxygen atoms. The first additional binding site seems to be quite special. The caesium ion is bound to the phenyl ring of a tryptophan residue. It is further liganded by two oxygen atoms. The third binding site is a result of crystal packing effects: caesium is liganded by four oxygen atoms, provided by two rhodanese molecules and one sulphate ion. It is likely that the binding of caesium affects the fluorescence of the tryptophan residue with which it interacts. Such possible effects should also be kept in mind when caesium ions are used as a quencher in fluorescence studies of proteins in general

Detergent organisation in crystals of monomeric outer membrane phospholipase A

The structure of the detergent in crystals of outer membrane phospholipase A (OMPLA) has been determined using neutron diffraction contrast variation. Large crystals were soaked in stabilising solutions, each containing a different H2O/D2O contrast. From the neutron diffraction at five contrasts, the 12 Å resolution structure of the detergent micelle around the protein molecule was determined. The hydrophobic β-barrel surfaces of the protein molecules are covered by rings of detergent. These detergent belts are fused to neighbouring detergent rings forming a continuous three-dimensional network throughout the crystal. The thickness of the detergent layer around the protein varies from 7–20 Å. The enzyme's active site is positioned just outside the hydrophobic detergent zone and is thus in a proper location to catalyse the hydrolysis of phospholipids in a natural membrane. Although the dimerisation face of OMPLA is covered with detergent, the detergent density is weak near the exposed polar patch, suggesting that burying this patch in the enzyme's dimer interface may be energetically favourable. Furthermore, these results indicate a crucial role for detergent coalescence during crystal formation and contribute to the understanding of membrane protein crystallisation.

Structural investigations of calcium binding and its role in activity and activation of outer membrane phospholipase A from Escherichia coli

Outer membrane phospholipase A (OMPLA) is an integral membrane enzyme that catalyses the hydrolysis of phospholipids. Enzymatic activity is regulated by reversible dimerisation and calcium-binding. We have investigated the role of calcium by X-ray crystallography. In monomeric OMPLA, one calcium ion binds between two external loops (L3L4 site) at 10 Angstrom from the active site. After dimerisation, a new calcium-binding site (catalytic site) is formed at the dimer interface in the active site of each molecule at 6 Angstrom from the L3L4 calcium site. The close spacing and the difference in calcium affinity of both sites suggests that the L3L4 site may function as a storage site for a calcium ion, which relocates to the catalytic site upon dimerisation. A. sequence alignment demonstrates conservation of the catalytic calcium site but evolutionary variation of the L3L4 site. The residues in the dimer interface are conserved as well, suggesting that all outer membrane phospholipases require dimerisation and calcium in the catalytic site for activity. For this family of phospholipases, we have characterised a consensus sequence motif (YTQ-X-11-G-X-2 -H-X-SNG) that contains conserved residues involved in dimerisation and catalysis. (C) 2001 Academic Press