472 research outputs found

    Surface properties of SmB6 from x-ray photoelectron spectroscopy

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    We have investigated the properties of cleaved SmB6_6 single crystals by x-ray photoelectron spectroscopy. At low temperatures and freshly cleaved samples a surface core level shift is observed which vanishes when the temperature is increased. A Sm valence between 2.5 - 2.6 is derived from the relative intensities of the Sm2+^{2+} and Sm3+^{3+} multiplets. The B/Sm intensity ratio obtained from the core levels is always larger than the stoichiometric value. Possible reasons for this deviation are discussed. The B 1s1s signal shows an unexpected complexity: an anomalous low energy component appears with increasing temperature and is assigned to the formation of a suboxide at the surface. While several interesting intrinsic and extrinsic properties of the SmB6_6 surface are elucidated in this manuscript no clear indication of a trivial mechanism for the prominent surface conductivity is found

    Isolation and characterization of the herpes simplex virus 1 terminase complex

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    During herpes simplex virus 1 (HSV-1) infection, empty procapsids are assembled and subsequently filled with the viral genome by means of a protein complex called the terminase, which is comprised of the HSV-1 UL15, UL28, and UL33 proteins. Biochemical studies of the terminase proteins have been hampered by the inability to purify the intact terminase complex. In this study, terminase complexes were isolated by tandem-affinity purification (TAP) using recombinant viruses expressing either a full-length NTAP-UL28 fusion protein (vFH476) or a C-terminally truncated NTAP-UL28 fusion protein (vFH499). TAP of the UL28 protein from vFH476-infected cells, followed by silver staining, Western blotting, and mass spectrometry, identified the UL15, UL28, and UL33 subunits, while TAP of vFH499-infected cells confirmed previous findings that the C terminus of UL28 is required for UL28 interaction with UL33 and UL15. Analysis of the oligomeric state of the purified complexes by sucrose density gradient ultracentrifugation revealed that the three proteins formed a complex with a molecular mass that is consistent with the formation of a UL15-UL28-UL33 heterotrimer. In order to assess the importance of conserved regions of the UL15 and UL28 proteins, recombinant NTAP-UL28 viruses with mutations of the putative UL28 metal-binding domain or within the UL15 nuclease domain were generated. TAP of UL28 complexes from cells infected with each domain mutant demonstrated that the conserved cysteine residues of the putative UL28 metal-binding domain and conserved amino acids within the UL15 nuclease domain are required for the cleavage and packaging functions of the viral terminase, but not for terminase complex assembly

    The ‘dance’ of life: visualizing metamorphosis during pupation in the blow fly Calliphora vicina by X-ray video imaging and micro-computed tomography

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    © 2017 The Authors. Published by the Royal Society under the terms of the Creative Commons Attribution License http://creativecommons.org/licenses/by/4.0/, which permits unrestricted use, provided the original author and source are credited. The attached file is the published version of the article
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