| 1. |
- Casolino, M., et al.
(författare)
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Cosmic-ray observations of the heliosphere with the PAMELA experiment
- 2006
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Ingår i: Astrophysics. - : Elsevier BV. ; , s. 1848-1852
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Konferensbidrag (refereegranskat)abstract
- The PAMELA experiment is a multi-purpose apparatus built around a permanent magnet spectrometer, with the main goal of studying in detail the antiparticle component of cosmic rays. The apparatus will be carried in space by means of a Russian satellite, due to launch in 2005, for a three year-long mission. The characteristics of the detectors composing the instrument, alongside the long lifetime of the mission and the orbital characteristics of the satellite, will allow to address several items of cosmic-ray physics. In this paper, we will focus on the solar and heliospheric observation capabilities of PAMELA.
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| 2. |
- Stozhkov, Y. I., et al.
(författare)
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About Separation of Hadron and Electromagnetic Cascades in the Pamela Calorimeter
- 2005
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Ingår i: International Journal of Modern Physics A. - 0217-751X .- 1793-656X. ; 20:29, s. 6745-6748
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Tidskriftsartikel (refereegranskat)abstract
- Results of calibration of the PAMELA instrument at the CERN facilities are discussed. In September, 2003, the calibration of the Neutron Detector together with the Calorimeter was performed with the CERN beams of electrons and protons with energies of 20-180 GeV. The implementation of the Neutron Detector increases a rejection factor of hadrons from electrons about ten times. The results of calibration are in agreement with calculations.
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| 3. |
- Andersson, V., et al.
(författare)
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Large-Area Balloon-Borne Polarized Gamma Ray Observer (PoGO)
- 2005
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Ingår i: Proceedings of the 22nd Texas Symposium on Relativistic Astrophysics at Stanford. ; , s. 736-743
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Konferensbidrag (refereegranskat)abstract
- We are developing a new balloon-borne instrument (PoGO), to measure polarization of soft gamma rays (30-200 keV) using asymmetry in azimuth angle distribution of Compton scattering. PoGO is designed to detect 10 % polarization in 100mCrab sources in a 6-8 hour observation and bring a new dimension to studies on gamma ray emission/transportation mechanism in pulsars, AGNs, black hole binaries, and neutron star surface. The concept is an adaptation to polarization measurements of well-type phoswich counter consisting of a fast plastic scintillator (the detection part), a slow plastic scintillator (the active collimator) and a BGO scintillator (the bottom anti-counter). PoGO consists of close-packed array of 217 hexagonal well-type phoswich counters and has a narrow field-of-view (~ 5 deg2) to reduce possible source confusion. A prototype instrument has been tested in the polarized soft gamma-ray beams at Advanced Photon Source (ANL) and at Photon Factory (KEK). On the results, the polarization dependence of EGS4 has been validated and that of Geant4 has been corrected.
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| 4. |
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| 5. |
- Cioci, Gianluca, et al.
(författare)
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Beta-propeller crystal structure of Psathyrella velutina lectin: an integrin-like fungal protein interacting with monosaccharides and calcium.
- 2006
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Ingår i: Journal of molecular biology. - : Elsevier BV. - 0022-2836 .- 1089-8638. ; 357:5, s. 1575-91
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Tidskriftsartikel (refereegranskat)abstract
- The lectin from the mushroom Psathyrella velutina recognises specifically N-acetylglucosamine and N-acetylneuraminic acid containing glycans. The crystal structure of the 401 amino acid residue lectin shows that it adopts a very regular seven-bladed beta-propeller fold with the N-terminal region tucked into the central cavity around the pseudo 7-fold axis. In the complex with N-acetylglucosamine, six monosaccharides are bound in pockets located between two consecutive propeller blades. Due to the repeats shown by the sequence the binding sites are very similar. Five hydrogen bonds between the protein and the sugar hydroxyl and N-acetyl groups stabilize the complex, together with the hydrophobic interactions with a conserved tyrosine and histidine. The complex with N-acetylneuraminic acid shows molecular mimicry with the same hydrogen bond network, but with different orientations of the carbohydrate ring in the binding site. The beta-hairpin loops connecting the two inner beta-strands of each blade are metal binding sites and two to three calcium ions were located in the structure. The multispecificity and high multivalency of this mushroom lectin, combined with its similarity to the extracellular domain of an important class of cell adhesion molecules, integrins, are another example of the outstanding success of beta-propeller structures as molecular binding machines in nature.
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| 6. |
- Kostlánová, Nikola, et al.
(författare)
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The fucose-binding lectin from Ralstonia solanacearum. A new type of beta-propeller architecture formed by oligomerization and interacting with fucoside, fucosyllactose, and plant xyloglucan.
- 2005
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Ingår i: The Journal of biological chemistry. - : Elsevier BV. - 0021-9258 .- 1083-351X. ; 280:30, s. 27839-49
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Tidskriftsartikel (refereegranskat)abstract
- Plant pathogens, like animal ones, use protein-carbohydrate interactions in their strategy for host recognition, attachment, and invasion. The bacterium Ralstonia solanacearum, which is distributed worldwide and causes lethal wilt in many agricultural crops, was shown to produce a potent L-fucose-binding lectin, R. solanacearum lectin, a small protein of 90 amino acids with a tandem repeat in its amino acid sequence. In the present study, surface plasmon resonance experiments conducted on a series of oligosaccharides show a preference for binding to alphaFuc1-2Gal and alphaFuc1-6Gal epitopes. Titration microcalorimetry demonstrates the presence of two binding sites per monomer and an unusually high affinity of the lectin for alphaFuc1-2Gal-containing oligosaccharides (KD = 2.5 x 10(-7) M for 2-fucosyllactose). R. solanacearum lectin has been crystallized with a methyl derivative of fucose and with the highest affinity ligand, 2-fucosyllactose. X-ray crystal structures, the one with alpha-methyl-fucoside being at ultrahigh resolution, reveal that each monomer consists of two small four-stranded anti-parallel beta-sheets. Trimerization through a 3-fold or pseudo-3-fold axis generates a six-bladed beta-propeller architecture, very similar to that previously described for the fungal lectin of Aleuria aurantia. This is the first report of a beta-propeller formed by oligomerization and not by sequential domains. Each monomer presents two fucose binding sites, resulting in six symmetrically arranged sugar binding sites for the beta-propeller. Crystals were also obtained for a mutated lectin complexed with a fragment of xyloglucan, a fucosylated polysaccharide from the primary cell wall of plants, which may be the biological target of the lectin.
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