| 1. |
- da Silva Santos, João Manuel, et al.
(författare)
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ALMA observations of transient heating in a solar active region
- 2020
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Ingår i: Astronomy and Astrophysics. - : EDP Sciences. - 0004-6361 .- 1432-0746. ; 643
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Tidskriftsartikel (refereegranskat)abstract
- Aims. We aim to investigate the temperature enhancements and formation heights of solar active-region brightenings such as Ellerman bombs (EBs), ultraviolet bursts (UVBs), and flaring active-region fibrils (FAFs) using interferometric observations in the millimeter (mm) continuum provided by the Atacama Large Millimeter/submillimeter Array (ALMA).Methods. We examined 3 mm signatures of heating events identified in Solar Dynamics Observatory observations of an active region and compared the results with synthetic spectra from a 3D radiative magnetohydrodynamic simulation. We estimated the contribution from the corona to the mm brightness using differential emission measure analysis.Results. We report the null detection of EBs in the 3 mm continuum at ∼1.2″ spatial resolution, which is evidence that they are sub-canopy events that do not significantly contribute to heating the upper chromosphere. In contrast, we find the active region to be populated with multiple compact, bright, flickering mm-bursts – reminiscent of UVBs. The high brightness temperatures of up to ∼14 200 K in some events have a contribution (up to ∼7%) from the corona. We also detect FAF-like events in the 3 mm continuum. These events show rapid motions of > 10 kK plasma launched with high plane-of-sky velocities (37 − 340 km s−1) from bright kernels. The mm FAFs are the brightest class of warm canopy fibrils that connect magnetic regions of opposite polarities. The simulation confirms that ALMA should be able to detect the mm counterparts of UVBs and small flares and thus provide a complementary diagnostic for localized heating in the solar chromosphere.
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| 2. |
- Hall, Michael, et al.
(författare)
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Structural basis for glutathione-mediated activation of the virulence regulatory protein PrfA in Listeria
- 2016
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Ingår i: Proceedings of the National Academy of Sciences of the United States of America. - : Proceedings of the National Academy of Sciences. - 0027-8424 .- 1091-6490. ; 113:51, s. 14733-14738
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Tidskriftsartikel (refereegranskat)abstract
- Infection by the human bacterial pathogen Listeria monocytogenes is mainly controlled by the positive regulatory factor A (PrfA), a member of the Crp/Fnr family of transcriptional activators. Published data suggest that PrfA requires the binding of a cofactor for full activity, and it was recently proposed that glutathione (GSH) could fulfill this function. Here we report the crystal structures of PrfA in complex with GSH and in complex with GSH and its cognate DNA, the hly operator PrfA box motif. These structures reveal the structural basis for a GSH-mediated allosteric mode of activation of PrfA in the cytosol of the host cell. The crystal structure of PrfAWT in complex only with DNA confirms that PrfAWT can adopt a DNA binding-compatible structure without binding the GSH activator molecule. By binding to PrfA in the cytosol of the host cell, GSH induces the correct fold of the HTH motifs, thus priming the PrfA protein for DNA interaction.
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| 3. |
- Hall, Michael, et al.
(författare)
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Structure of the C-terminal domain of AspA (antigen I/II-family) protein from Streptococcus pyogenes
- 2014
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Ingår i: FEBS Open Bio. - : Elsevier. - 2211-5463. ; 4, s. 283-289
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Tidskriftsartikel (refereegranskat)abstract
- The pathogenic bacteria Streptococcus pyogenes can cause an array of diseases in humans, including moderate infections such as pharyngitis (strep throat) as well as life threatening conditions such as necrotizing fasciitis and puerperal fever. The antigen I/II family proteins are cell wall anchored adhesin proteins found on the surfaces of most oral streptococci and are involved in host colonization and biofilm formation. In the present study we have determined the crystal structure of the C2–3-domain of the antigen I/II type protein AspA from S. pyogenes M type 28. The structure was solved to 1.8 Å resolution and shows that the C2–3-domain is comprised of two structurally similar DEv-IgG motifs, designated C2 and C3, both containing a stabilizing covalent isopeptide bond. Furthermore a metal binding site is identified, containing a bound calcium ion. Despite relatively low sequence identity, interestingly, the overall structure shares high similarity to the C2–3-domains of antigen I/II proteins from Streptococcus gordonii and Streptococcus mutans, although certain parts of the structure exhibit distinct features. In summary this work constitutes the first step in the full structure determination of the AspA protein from S. pyogenes.
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| 4. |
- Hol, Jeroen, et al.
(författare)
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Modeling and Calibration of Inertial and Vision Sensors
- 2009
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Rapport (övrigt vetenskapligt/konstnärligt)abstract
- This paper is concerned with the problem of estimating the relative translation and orientation of an inertial measurement unit and a camera, which are rigidly connected. The key is to realize that this problem is in fact an instance of a standard problem within the area of system identification, referred to as a gray-box problem. We propose a new algorithm for estimating the relative translation and orientation, which does not require any additional hardware, except a piece of paper with a checkerboard pattern on it. The method is based on a physical model which can also be used in solving, for example, sensor fusion problems. The experimental results show that the method works well in practice, both for perspective and spherical cameras.
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