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We present major elements compositions and volatiles contents of olivine-hosted melt inclusions from Etna volcano (Italy), which extend the existing database with the aim of interpreting the chemical variability of Etnean magmas over the last 15 ka. Olivine phenocrysts were selected from the most primitive Fall Stratified (FS) eruptive products of picritic composition (Mg# = 67–70, Fo89–91), the Mt. Spagnolo eccentric lavas (Mg# = 52–64, Fo82–88) and among the more recent 2002–2013 eruptive products (Mg# = 33–53, Fo68–83). Crystal fractionation and degassing processes were modeled at temperatures of 1050–1300 °C, pressures <500 MPa, and oxygen fugacity between 1 and 2 log units above the nickel-nickel oxide buffer, in order to interpret melt inclusions data. Melt inclusions show a great variability in major elements chemistry (e.g., 44–57 wt% SiO2, 3–16 wt% CaO, 4–13 wt% FeO, 2–12 wt% MgO, 1–6 wt% K2O), designating a continuous differentiation trend from FS toward 2013 entrapped melts, which is mostly reproduced by the fractional crystallization of olivine + spinel + clinopyroxene ± plagioclase, in order of appearance. Volatile contents in the glass inclusions are also extremely variable, with maxima up to 6 wt% H2O and 0.6 wt% CO2 in FS melt inclusions, and up to 0.43 wt% S in Mt. Spagnolo inclusions. H2O and CO2 contents in the melt inclusions suggest minimum entrapment depths of 4–19 km (below crater level) for FS inclusions and <10 km for the 2002–2013 trachybasalts. Petrological arguments coupled to the modeling of fractional crystallization and degassing processes concur to suggest that magmas from Mt. Spagnolo and the recent eruptions may be produced by differentiation from the most primitive volatile-rich FS magma along variable P-T paths, occasionally accompanied by secondary processes as crustal assimilation, mixing, and CO2 flushing. We do not exclude the occurrence of source processes at Etna, e.g., variable degrees of mantle melting and/or variabl

Our seismic tomographic images characterize, for the first time, spatial and volumetric details of the subvertical magma plumbing system of Merapi Volcano. We present P-and S-wave arrival time data, which were collected in a dense seismic network, known as DOMERAPI, installed around the volcano for 18 months. The P-and S-wave arrival time data with similar path coverage reveal a high Vp/Vs structure extending from a depth of >= 20 km below mean sea level (MSL) up to the summit of the volcano. Combined with results of petrological studies, our seismic tomography data allow us to propose: (1) the existence of a shallow zone of intense fluid percolation, directly below the summit of the volcano; (2) a main, pre-eruptive magma reservoir at >= 10 to 20 km below MSL that is orders of magnitude larger than erupted magma volumes; (3) a deep magma reservoir at MOHO depth which supplies the main reservoir; and (4) an extensive, subvertical fluid-magma-transfer zone from the mantle to the surface. Such high-resolution spatial constraints on the volcano plumbing system as shown are an important advance in our ability to forecast and to mitigate the hazard potential of Merapi's future eruptions.

© 2018 Elsevier Inc. The Gram-positive bacterium Bacillus subtilis responds to starvation by entering a morphological differentiation process leading to the formation of a highly resistant spore. Early in the sporulation process, the cell asymmetrically divides into a large compartment (the mother cell) and a smaller one (the forespore), which will maturate into a resistant spore. Proper development of the forespore requires the assembly of a multiprotein complex called the SpoIIIA-SpoIIQ complex or “A-Q complex”. This complex involves the forespore protein SpoIIQ and eight mother cell proteins (SpoIIIAA to SpoIIIAH), many of which share structural similarities with components of specialized secretion systems and flagella found in Gram-negative bacteria. The assembly of the A-Q complex across the two membranes that separate the mother cell and forespore was recently shown to require GerM. GerM is a lipoprotein composed of two GerMN domains, a family of domains with unknown function. Here, we report X-ray crystallographic structures of the first GerMN domain of GerM at 1.0 Å resolution, and of the soluble domain of GerM (the tandem of GerMN domains) at 2.1 Å resolution. These structures reveal that GerMN domains can adopt distinct conformations and that the core of these domains display structural similarities with ring-building motifs found in components of specialized secretion system and in SpoIIIA proteins. This work provides an additional piece towards the structural characterization of the A-Q complex.