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Between Aug. 2014 and Sept. 2016, while ESA's cornerstone mission Rosetta was operating in the vicinity of the nucleus and in the coma of comet 67P/Churyumov-Gerasimenko, the COSIMA instrument collected a large number of dust particles with diameters up to a millimeter. Positive or negative ions were detected by a time-of-flight secondary ion mass spectrometer (TOF-SIMS) and the composition of selected particles was deduced. Many of the negative ion mass spectra show, besides mass peaks at the correct position, an additional, extended contribution at the lower mass side caused by partial charging of the dust. This effect, usually avoided in SIMS applications, can in our case be used to obtain information on the electrical properties of the collected cometary dust particles, such as the specific resistivity (ρr>1.2⋅1010Ωm) and the real part of the relative electrical permittivity (εr<1.2). From these values a lower limit for the porosity is derived (P>0.8)., Funding details: Austrian Science Fund, FWF, P26871-N20; Funding details: Centre National d’Etudes Spatiales, CNES; Funding details: Deutsches Zentrum für Luft- und Raumfahrt, DLR, 50 QP 1801; Funding text 1: COSIMA was built by a consortium led by the Max-Planck-Institut für Extraterrestrische Physik, Garching, Germany in collaboration with Laboratoire de Physique et Chimie de l’Environnement et de l’Espace, Orléans, France, Institut d’Astrophysique Spatiale, CNRS/Université Paris Sud, Orsay, France, Finnish Meteorological Institute, Helsinki, Finland, Universität Wuppertal, Wuppertal, Germany, von Hoerner und Sulger GmbH, Schwetzingen, Germany, Universität der Bundeswehr München, Neubiberg, Germany, Institut für Physik, Forschungszentrum Seibersdorf, Seibersdorf, Austria, Institut für Weltraumforschung, Österreichische Akademie der Wissenschaften, Graz, Austria and is lead by the Max-Planck-Institut für Sonnensystemforschung, Göttingen, Germany. The support of the national funding agencies of Germany ( DLR , grant 50 QP 1801 ), France ( CNES ), Austria ( FWF , grant P26871-N20 ), Finland and the ESA Technical Directorate is gratefully acknowledged. We thank the Rosetta Science Ground Segment at ESAC, the Rosetta Mission Operations Centre at ESOC and the Rosetta Project at ESTEC for their outstanding work enabling the science return of the Rosetta Mission. Appendix A

Azole-resistant strains of Aspergillus fumigatus have been detected and the underlying molecular mechanisms of resistance characterized. Point mutations in the cyp51A gene have been proved to be related to azole resistance in A. fumigatus clinical strains and with different resistance profiles depending on the amino acid change (G54E, G54V, G54R, G54W, M220V, M220K, M220T, M220I). The aim of this work was to express A. fumigatus cyp51A genes in the yeast Saccharomyces cerevisiae in order to better assess the contribution of each independent amino acid substitution to resistance. A tetracycline regulatable system allowing repression of the endogenous essential ERG11 gene was used. The expression of Aspergillus cyp51A alleles could efficiently restore the absence of ERG11 in S. cerevisiae. In general, S. cerevisiae clones expressing. A. fumigatus cyp51A alleles from azole-resistant isolates showed higher MICs to all azoles tested than those expressing alleles from susceptible isolates. The azole susceptibility profiles obtained in S. cerevisiae upon expression of specific cyp51A alleles recapitulated susceptibility profiles observed from their A. fumigatus origins. In conclusion this work supports the concept that characteristics of specific A. fumigatus cyp51A alleles could be investigated in the heterologous host S. cerevisiae

Evolved resistance to fungicides is a major problem limiting our ability to control agricultural, medical and veterinary pathogens and is frequently associated with substitutions in the amino acid sequence of the target protein. The convention for describing amino acid substitutions is to cite the wild-type amino acid, the codon number and the new amino acid, using the one-letter amino acid code. It has frequently been observed that orthologous amino acid mutations have been selected in different species by fungicides from the same mode of action class, but the amino acids have different numbers. These differences in numbering arise from the different lengths of the proteins in each species. The purpose of the present paper is to propose a system for unifying the labelling of amino acids in fungicide target proteins. To do this we have produced alignments between fungicide target proteins of relevant species fitted to a well-studied ‘archetype’ species. Orthologous amino acids in all species are then assigned numerical ‘labels’ based on the position of the amino acid in the archetype protein.

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