Rethinking media responsibility in the refugee ‘crisis’: a visual typology of European news

In this paper, we analyse how news images of the 2015 Syrian refugee ‘crisis’ visualise refugees and how, in so doing, they mobilise various forms of moral responsibility in ‘our’ mediated public life – various practical dispositions of action towards the misfortunes of migrants and refugees at Europe’s border. On the basis of empirical material from European news (June-December 2015), we construct a typology of visibilities of the ‘crisis’, each of which situates refugees within a different regime of visibility and claim to action: i) visibility as biological life, associated with monitorial action; ii) visibility as empathy associated with charitable action; iii) visibility as threat, associated with state security; iv) visibility as hospitality, associated with political activism; and v) visibility as selfreflexivity, associated with a post-humanitarian engagement with people like ‘us’. In conclusion, we argue that, important as these five categories of visibility are in introducing public dispositions to action towards the vulnerable, they nonetheless ultimately fail to humanise migrants and refugees. This failure to portray them as human beings with lives that are worth sharing should compel us, we urge, to radically re-think how we understand the media’s responsibility towards vulnerable others

A Multilaboratory Comparison of Calibration Accuracy and the Performance of External References in Analytical Ultracentrifugation

Analytical ultracentrifugation (AUC) is a first principles based method to determine absolute sedimentation coefficients and buoyant molar masses of macromolecules and their complexes, reporting on their size and shape in free solution. The purpose of this multi-laboratory study was to establish the precision and accuracy of basic data dimensions in AUC and validate previously proposed calibration techniques. Three kits of AUC cell assemblies containing radial and temperature calibration tools and a bovine serum albumin (BSA) reference sample were shared among 67 laboratories, generating 129 comprehensive data sets. These allowed for an assessment of many parameters of instrument performance, including accuracy of the reported scan time after the start of centrifugation, the accuracy of the temperature calibration, and the accuracy of the radial magnification. The range of sedimentation coefficients obtained for BSA monomer in different instruments and using different optical systems was from 3.655 S to 4.949 S, with a mean and standard deviation of (4.304 ± 0.188) S (4.4%). After the combined application of correction factors derived from the external calibration references for elapsed time, scan velocity, temperature, and radial magnification, the range of s-values was reduced 7-fold with a mean of 4.325 S and a 6-fold reduced standard deviation of ± 0.030 S (0.7%). In addition, the large data set provided an opportunity to determine the instrument-to-instrument variation of the absolute radial positions reported in the scan files, the precision of photometric or refractometric signal magnitudes, and the precision of the calculated apparent molar mass of BSA monomer and the fraction of BSA dimers. These results highlight the necessity and effectiveness of independent calibration of basic AUC data dimensions for reliable quantitative studies

A multilaboratory comparison of calibration accuracy and the performance of external references in analytical ultracentrifugation.

Analytical ultracentrifugation (AUC) is a first principles based method to determine absolute sedimentation coefficients and buoyant molar masses of macromolecules and their complexes, reporting on their size and shape in free solution. The purpose of this multi-laboratory study was to establish the precision and accuracy of basic data dimensions in AUC and validate previously proposed calibration techniques. Three kits of AUC cell assemblies containing radial and temperature calibration tools and a bovine serum albumin (BSA) reference sample were shared among 67 laboratories, generating 129 comprehensive data sets. These allowed for an assessment of many parameters of instrument performance, including accuracy of the reported scan time after the start of centrifugation, the accuracy of the temperature calibration, and the accuracy of the radial magnification. The range of sedimentation coefficients obtained for BSA monomer in different instruments and using different optical systems was from 3.655 S to 4.949 S, with a mean and standard deviation of (4.304 ± 0.188) S (4.4%). After the combined application of correction factors derived from the external calibration references for elapsed time, scan velocity, temperature, and radial magnification, the range of s-values was reduced 7-fold with a mean of 4.325 S and a 6-fold reduced standard deviation of ± 0.030 S (0.7%). In addition, the large data set provided an opportunity to determine the instrument-to-instrument variation of the absolute radial positions reported in the scan files, the precision of photometric or refractometric signal magnitudes, and the precision of the calculated apparent molar mass of BSA monomer and the fraction of BSA dimers. These results highlight the necessity and effectiveness of independent calibration of basic AUC data dimensions for reliable quantitative studies

epsilon-Crystallin from duck eye lens. Comparisonof its quaternary structure and stability with other lactate dehydrogenases and complex formation with alpha-crystallin

Taxon-specific {epsilon}-crystallin ({epsilon}C) from duck eye lens is identical to duck heart muscle lactate dehydrogenase. It forms a dimer of dimers with a dissociation constant of 2.2 x 10 -7 M, far beyond the value observed for other vertebrate lactate dehydrogenases. Comparing the characteristics of wild-type {epsilon}-crystallin with those of three mutants, G115N, G119F and 115N/119F, representing the only significant peripheral sequence variations between duck {epsilon}C and chicken or pig heart muscle lactate dehydrogenase, no significant conformational differences are detectable. Regarding the catalytic properties, the Michaelis constant of the double mutant 115N/119F for pyruvate is found to be decreased; for wild-type enzyme, the effect is overcompensated by the high expression level of {epsilon}C in the eye lens. As taken from spectral analysis of the guanidine-induced and temperature-induced denaturation transitions, {epsilon}C in its dimeric state is relatively unstable, whereas the native tetramer exhibits the high intrinsic stability characteristic of common vertebrate heart and muscle lactate dehydrogenases. The denaturation mechanism of {epsilon}C is complex and only partially reversible. In the case of thermal unfolding, the predominant side reaction competing with the reconstitution of the native state is the kinetic partitioning between proper folding and aggregation, {alpha}-Crystallin, the major molecular chaperone in the eye lens, inhibits the aggregation of {epsilon}C by trapping the misfolded protein