Monitoring hiring discrimination through online recruitment platforms.

Women (compared to men) and individuals from minority ethnic groups (compared to the majority group) face unfavourable labour market outcomes in many economies1,2, but the extent to which discrimination is responsible for these effects, and the channels through which they occur, remain unclear3,4. Although correspondence tests5-in which researchers send fictitious CVs that are identical except for the randomized minority trait to be tested (for example, names that are deemed to sound 'Black' versus those deemed to sound 'white')-are an increasingly popular method to quantify discrimination in hiring practices6,7, they can usually consider only a few applicant characteristics in select occupations at a particular point in time. To overcome these limitations, here we develop an approach to investigate hiring discrimination that combines tracking of the search behaviour of recruiters on employment websites and supervised machine learning to control for all relevant jobseeker characteristics that are visible to recruiters. We apply this methodology to the online recruitment platform of the Swiss public employment service and find that rates of contact by recruiters are 4-19% lower for individuals from immigrant and minority ethnic groups, depending on their country of origin, than for citizens from the majority group. Women experience a penalty of 7% in professions that are dominated by men, and the opposite pattern emerges for men in professions that are dominated by women. We find no evidence that recruiters spend less time evaluating the profiles of individuals from minority ethnic groups. Our methodology provides a widely applicable, non-intrusive and cost-efficient tool that researchers and policy-makers can use to continuously monitor hiring discrimination, to identify some of the drivers of discrimination and to inform approaches to counter it.

All-liquid dual-lens optofluidic zoom system.

An all-liquid optical zoom system based on two independently controllable liquid lenses positioned inside a single sealed cylindrical housing is demonstrated. This system yielded a zoom ratio of 1.5 for an object distance of 200 mm, an image distance 37 mm, and a corresponding resolution of better than 5 line pairs/mm. With a diameter of 5 mm, a packaged system length of 9.88 mm, and a power consumption of 3.5 mW, the system represents a new generation of ultra-miniaturized optofluidic systems with high functionality, excellent imaging properties, and highly flexible tunability, all with no mechanically moving parts.

Tubular astigmatism-tunable fluidic lens.

We demonstrate a new means to fabricate three-dimensional liquid lenses which may be tuned in focal length and astigmatism. Using actuation by electrowetting-on-dielectrics, astigmatism in arbitrary directions may be tuned independently, with almost no cross talk between orthogonal orientations. The lens is based on electrodes structured on planar polyimide foils and subsequently rolled, enabling high-resolution patterning of complex electrodes along the azimuthal and radial directions of the lens. Based on a design established through fluidic and optical simulations, the astigmatism tuning is experimentally verified by a change of the corresponding Zernike coefficients measured using a Shack-Hartmann wavefront sensor. It was seen that the back focal length can be tuned by 5 mm and 0° and 45° astigmatism by 3 µm through application of voltages in the range of 50 Vrms. It was observed that the cross talk with other aberrations is very low, suggesting a novel means for astigmatism control in imaging systems.

Optofluidic laser scanner based on a rotating liquid prism.

We demonstrate an electrowetting-actuated optofluidic system based on a rotatable liquid prism implemented as a two-dimensional laser scanner. The system is fabricated through a novel technology using a patterned flexible polymeric foil on which a high density of electrodes is structured and which is subsequently inserted into a cylindrical housing. The resulting radial electrode array is used for electrowetting actuation of two fluids filled into the cylinder, which allows a controllable tilt and orientation of the planar liquid interface and thus represents a tunable rotating prism. Finite element simulations and subsequent experimental verification show that this highly planar and precisely positionable liquid/liquid interface may be actuated to a deflection angle of ±6.4°, with a standard deviation of ±0.18°, and rotated 360° about the vertical axis. Power consumption is limited to several microwatts, and switching times of several hundred milliseconds were determined.

Microbial Carbonation of Monocalcium Silicate.

Biocement formed through microbially induced calcium carbonate precipitation (MICP) is an emerging biotechnology focused on reducing the environmental impact of concrete production. In this system, CO2 species are provided via ureolysis by Sporosarcina pasteurii (S. pasteurii) to carbonate monocalcium silicate for MICP. This is one of the first studies of its kind that uses a solid-state calcium source, while prior work has used highly soluble forms. Our study focuses on microbial physiological, chemical thermodynamic, and kinetic studies of MICP. Monocalcium silicate incongruently dissolves to form soluble calcium, which must be coupled with CO2 release to form calcium carbonate. Chemical kinetic modeling shows that calcium solubility is the rate-limiting step, but the addition of organic acids significantly increases the solubility, enabling extensive carbonation to proceed up to 37 mol %. The microbial urease activity by S. pasteurii is active up to pH 11, 70 °C, and 1 mol L-1 CaCl2, producing calcite as a means of solidification. Cell-free extracts are also effective albeit less robust at extreme pH, producing calcite with different physical properties. Together, these data help determine the chemical, biological, and thermodynamic parameters critical for scaling microbial carbonation of monocalcium silicate to high-density cement and concrete.

A Prospective Study of Quantitative SPECT/CT for Evaluation of Lung Shunt Fraction Before SIRT of Liver Tumors.

The lung shunt fraction (LSF) is estimated using 99mTc-macroaggregated albumin (99mTc-MAA) imaging before selective internal radiotherapy (SIRT) of the liver to reduce the risk of pulmonary irradiation. Generally, planar scans are acquired after injection of 99mTc-MAA into the hepatic artery. However, the validity of this approach is limited by differences in attenuation between liver and lung tissue as well as inaccurate segmentation of the organs. The aim of this study was to evaluate quantitative SPECT/CT for LSF assessment in a prospective clinical cohort. Methods: Fifty consecutive patients intended to undergo SIRT were imaged within 1 h after injection of 99mTc-MAA using a SPECT/CT γ-camera. Planar scans of the lung and liver region were acquired in anterior and posterior views, followed by SPECT/CT scans of the thorax and abdomen. Emission data were corrected for scatter, attenuation, and resolution recovery using dedicated software. To quantify the radioactivity concentration in the lung, liver, urinary bladder and remainder of the thoracoabdominal body, volumes of interest were defined on the SPECT/CT images. 99mTc-MAA concentrations were calculated as percentage injected dose (%ID). Results: Mean 99mTc-MAA uptake in liver and lung accounted for only 79 %ID, whereas 13.1 %ID was present in the remainder of the body. In all patients, LSF as calculated from planar scans accounted for a median of 6.8% (range, 3.4%-32.3%), whereas the SPECT/CT quantitation revealed significantly lower LSF estimates, at a median of 1.9% (range, 0.8%-15.7%) (P < 0.0001, Wilcoxon test). On the basis of planar imaging, dose reduction or even contraindications to SIRT had to be considered in 10 of 50 patients, as their LSF was calculated at 10% or more. In contrast, SPECT/CT quantitation showed substantial shunting in only 2 of the 50 patients. Conclusion: Quantitative SPECT/CT reveals that the LSF is considerably lower than shown on planar imaging. Thus, the resulting dose to the lung parenchyma may be less than conventionally assumed. However, the safety of the SPECT/CT-derived dose range will have to be evaluated.

Soluble methane monooxygenase: activation of dioxygen and methane.

The mechanisms by which soluble methane monooxygenase uses dioxygen to convert methane selectively to methanol have come into sharp focus. Diverse techniques have clarified subtle details about each step in the reaction, from binding and activating dioxygen, to hydroxylation of alkanes and other substrates, to the electron transfer events required to complete the catalytic cycle.

Dioxygen Activation and Methane Hydroxylation by Soluble Methane Monooxygenase: A Tale of Two Irons and Three Proteins.

Methanotrophic bacteria are capable of using methane as their sole source of carbon and energy. The first step in methane metabolism, the oxidation of methane to methanol, is catalyzed by a fascinating enzyme system called methane monooxygenase (MMO). The selective oxidation of the very stable C-H bond in methane under ambient conditions is a remarkable feat that has not yet been repeated by synthetic catalysts and has attracted considerable scientific and commercial interest. The best studied MMO is a complex enzyme system that consists of three soluble protein components, all of which are required for efficient catalysis. Dioxygen activation and subsequent methane hydroxylation are catalyzed by a hydroxylase enzyme that contains a non-heme diiron site. A reductase protein accepts electrons from NADH and transfers them to the hydroxylase where they are used for the reductive activation of O2 . The third protein component couples electron and dioxygen consumption with methane oxidation. In this review we examine different aspects of catalysis by the MMO proteins, including the mechanisms of dioxygen activation at the diiron site and substrate hydroxylation by the activated oxygen species. We also discuss the role of complex formation between the different protein components in regulating various aspects of catalysis.

Dioxygen Activation and Methane Hydroxylation by Soluble Methane Monooxygenase: A Tale of Two Irons and Three Proteins A list of abbreviations can be found in Section 7.

Methanotrophic bacteria are capable of using methane as their sole source of carbon and energy. The first step in methane metabolism, the oxidation of methane to methanol, is catalyzed by a fascinating enzyme system called methane monooxygenase (MMO). The selective oxidation of the very stable C-H bond in methane under ambient conditions is a remarkable feat that has not yet been repeated by synthetic catalysts and has attracted considerable scientific and commercial interest. The best studied MMO is a complex enzyme system that consists of three soluble protein components, all of which are required for efficient catalysis. Dioxygen activation and subsequent methane hydroxylation are catalyzed by a hydroxylase enzyme that contains a non-heme diiron site. A reductase protein accepts electrons from NADH and transfers them to the hydroxylase where they are used for the reductive activation of O(2). The third protein component couples electron and dioxygen consumption with methane oxidation. In this review we examine different aspects of catalysis by the MMO proteins, including the mechanisms of dioxygen activation at the diiron site and substrate hydroxylation by the activated oxygen species. We also discuss the role of complex formation between the different protein components in regulating various aspects of catalysis.

Optofluidic router based on tunable liquid-liquid mirrors.

We present an electrically tunable 1 × 5 optofluidic router for on-chip light routing. The device can redirect light from an optical input channel into five output channels by exploiting total internal reflection (TIR) at a liquid-liquid interface. The liquid-liquid mirrors, demonstrated for the first time, are tuned using integrated electrowetting-on-dielectrics (EWOD) actuators. The router is assembled from two chips fabricated by standard MEMS techniques. Through a combination of microfluidic with micro-optical components on chip, reliable light routing is achieved with switching times of [1.5-3.3] s, efficiencies of coupling into channels of up to 12%, optical cross-talk as low as -24 dB, a required drive voltage of 50 V, and a low power consumption of <5 mW, using a device 12 × 13 × 2 mm(3) in size. The optofluidic approach enables addressing of multiple channels over a broad wavelength range. Such optical routing capabilities are important for lab-on-chip devices focusing on optical spectroscopy, optical detection, or even optical manipulation. When integrated with external light sources and a low-cost disposable photonic lab-on-a-chip, the router could thus lead to novel laboratory measurement systems.

Development of metal nanocluster ion source based on dc magnetron plasma sputtering at room temperature.

A simple and cost effective nanocluster ion source for the deposition of size selected metal nanocluster has been developed based on the dc magnetron discharge (including pulsed dc discharge). The most important and interesting feature of this cluster source is that it is working at room temperature, cooled by chilled water during the experiment. There is no extraction unit in this device and the cluster streams flow only due to the pressure gradient from source chamber to substrate via quadrupole mass filter. It has provision of multiple substrate holders in the deposition chamber, which can be controlled manually. The facility consists of quadrupole mass filter (QMF 200), which can select masses in the range of 2-125 000 atoms depending on the target materials, with a constant mass resolution (M/DeltaM approximately 25). The dc magnetron discharge at a power of about 130 W with Ar as feed/buffer gas was used to produce the Cu nanocluster in an aggregation tube and deposited on Si (100) wafer temperature.

[Prevalence of psychiatric disorders in prisoners with a short imprisonment: results from a prison in north Germany]. / Die Prävalenz psychischer Erkrankungen bei Gefängnisinsassen mit Kurzzeitstrafe.

OBJECTIVE: The aim of the study was to determine the prevalence of mental disorders among prisoners with a short prison term. METHODS: We investigated 102 participants with the Structured Clinical Interview for DSM Disorders (SCID I and II) and the Symptom Check List (SCL-90). RESULTS: We found a lifetime-prevalence of mental disorders (axis I) of 83 %. 80 % of the participants showed at least one personality disorder. CONCLUSIONS: These results indicate that short-term prisoners are a population which is highly troubled in a psychiatric sense and shows a need of treatment in prison.

Structural features of covalently cross-linked hydroxylase and reductase proteins of soluble methane monooxygenase as revealed by mass spectrometric analysis.

Soluble methane monooxygenase requires complexes between its three component proteins for efficient catalysis. The hydroxylase (MMOH) must bind both to the reductase (MMOR) and to the regulatory protein (MMOB) to facilitate oxidation of methane to methanol. Although structures of MMOH, MMOB, and one domain of MMOR have been determined, less geometric information is available for the complexes. To address this deficiency, MMOH and MMOR were cross-linked by a carbodiimide reagent and analyzed by specific proteolysis, matrix-assisted laser desorption/ionization time-of-flight mass spectrometry, and capillary high performance liquid chromatography mass spectrometry. Tandem mass spectra conclusively identified two amine-to-carboxylate cross-linked sites involving the alpha subunit of MMOH and the [2Fe-2S] domain of MMOR (MMOR-Fd). In particular, the N terminus of the MMOH alpha subunit forms cross-links to the side chains of MMOR-Fd residues Glu-56 and Glu-91. These Glu residues are close to one another on the surface of MMOR-Fd and >25 A from the [2Fe-2S] cluster. Because the N terminus of the alpha subunit of MMOH was not located in the crystal structure of MMOH, a detailed structural model of the complex based on the cross-link was precluded; however, a previously proposed binding site for MMOR on MMOH could be ruled out. Based on the cross-linking results, a MMOR E56Q/E91Q double mutant was generated. The mutant retains >80% of MMOR NADH oxidase activity but reduces sMMO activity to approximately 65% of the level supported by the wild type reductase. Cross-linking to MMOH was diminished but not abolished in the double mutant, indicating that other residues of MMOR also form cross-links to MMOH.

Evaluation of norcarane as a probe for radicals in cytochome p450- and soluble methane monooxygenase-catalyzed hydroxylation reactions.

Norcarane was employed as a mechanistic probe in oxidations catalyzed by hepatic cytochome P450 enzymes and by the soluble methane monooxygenase (sMMO) enzyme from Methylococcuscapsulatus (Bath). In all cases, the major oxidation products (>75%) were endo- and exo-2-norcaranol. Small amounts of 3-norcaranols, 2-norcaranone, and 3-norcaranone also formed. In addition, the rearrangement products (2-cyclohexenyl)methanol and 3-cycloheptenol were detected in the reactions, the former possibly arising from a radical intermediate and the latter ascribed to a cationic intermediate. The formation of the cation-derived rearrangement product is consistent with one or more reaction pathways and is in accord with the results of previous probe studies with the same enzymes. The appearance of the putative radical-derived rearrangement product is in conflict with other mechanistic probe results with the same enzymes. The unique implication of a discrete radical intermediate in hydroxylations of norcarane may be the consequence of a minor reaction pathway for the enzymes that is not manifest in reactions with other probes. Alternatively, it might reflect a previously unappreciated reactivity of norcaranyl cationic intermediates, which can convert to (2-cyclohexenyl)methanol. We conclude that generalizations regarding the intermediacy of radicals in P450 and sMMO enzyme-catalyzed hydroxylations based on the norcarane results should be considered hypothetical until the origin of the unanticipated results can be determined.

Product binding to the diiron(III) and mixed-valence diiron centers of methane monooxygenase hydroxylase studied by (1,2)H and (19)F ENDOR spectroscopy.

The binding of ethanol and 1,1,1-trifluoroethanol (TFE) to both the H(mv) and H(ox) forms of soluble methane monooxygenase (sMMO) in solution has been studied by Q-band (35 GHz) CW and pulsed ENDOR spectroscopy of (1)H, (2)H and (19)F nuclei of exogenous ligands. As part of this investigation we introduce (19)F, in this case from bound TFE, as a new probe for the binding of small molecules to a metalloenzyme active site. The H(mv) form was prepared in solution by chemical reduction of H(ox). For study of H(ox) itself, frozen solutions were subjected to gamma-irradiation in the frozen solution state at 77 K, which affords an EPR-visible mixed-valent diiron center, denoted (H(ox))(mv), held in the geometry of the diiron(III) state. The (19)F and (2)H ENDOR spectra of bound TFE together with (1,2)H ENDOR spectra of bound ethanol indicate that the alcohols bind close to the Fe(II) ion of the mixed-valence cluster in H(mv) and in a bridging or semi-bridging fashion to H(ox). DMSO does not affect the binding of either of the ethanols or of methanol to H(ox), nor of ethanol or methanol to H(mv). It does, however, displace TFE from the diiron site in H(mv). These results provide the first evidence that crystal structures of sMMO hydroxylase into which product alcohols were introduced by diffusion represent the structures in solution.