Browsing by Subject "X-RAY-DIFFRACTION"

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  • Maksimova, A. A.; Petrova, E. V.; Chukin, A. V.; Karabanalov, M. S.; Felner, I.; Gritsevich, M.; Oshtrakh, M. I. (2020)
    We studied the interior and the fusion crust of the recently recovered Ozerki L6 meteorite using optical microscopy, scanning electron microscopy (SEM) with energy dispersive spectroscopy, X-ray diffraction (XRD), magnetization measurements, and Mossbauer spectroscopy. The phase composition of the interior and of the fusion crust was determined by means of SEM, XRD, and Mossbauer spectroscopy. The unit cell parameters for silicate crystals were evaluated from the X-ray diffractograms and were found the same for the interior and the fusion crust. Magnetization measurements revealed a decrease of the saturation magnetic moment in the fusion crust due to a decrease of Fe-Ni-Co alloy content. Both XRD and Mossbauer spectroscopy show the presence of magnesioferrite in the fusion crust. The temperatures of cation equilibrium distribution between the M1 and M2 sites in silicates calculated using the data obtained from XRD and Mossbauer spectroscopy appeared to be in a good consistency: 553 and 479 K for olivine and 1213 and 1202 K for orthopyroxene.
  • Ertbjerg, Per; Puolanne, Eero (2017)
    The basic contractile unit of muscle, the sarcomere, will contract as the muscle goes into rigor post-mortem. Depending on the conditions, such as the rate of pH decline, the cooling rate and the mechanical restraints on the muscles, this longitudinal shortening will result in various post-mortem sarcomere lengths as well as lateral differences in the distances between the myosin and actin filaments. This shortening is underlying the phenomena described as rigor contraction, thaw rigor, cold shortening and heat shortening. The shortening in combination with the molecular architecture of the sarcomere as defined by the myosin filaments and their S-1 and S-2 units, the interaction with the actin filaments, and the boundaries formed by the 2-disks will subsequently influence basic meat quality traits including tenderness and water-holding capacity. Biochemical reactions from proteolysis and glycogen metabolism interrelate with the sarcomere length in a complex manner. The sarcomere length is also influencing the eating quality of cooked meat and the water-holding in meat products.
  • Viitaja, Tuomo; Raitanen, Jan-Erik; Hynynen, Antti; Moilanen, Jukka; Svedström, Kirsi; Paananen, Riku O.; Ekholm, Filip S. (2022)
    The tear film lipid layer (TFLL) is important to the maintenance of ocular surface health. Surprisingly, information on the individual roles of the myriad of unique lipids found therein is limited. The most abundant lipid species are the wax esters (WE) and cholesteryl esters (CE), and, especially their branched analogs. The isolation of these lipid species from the TFLL has proved to be tedious, and as a result, insights on their biophysical profiles and role in the TFLL is currently lacking. Herein, we circumvent these issues by a total synthesis of the most abundant iso-methyl branched WEs and CEs found in the TFLL. Through a detailed characterization of the biophysical properties, by the use of Langmuir monolayer and wide-angle X-ray scattering techniques, we demonstrate that chain branching alters the behavior of these lipid species on multiple levels. Taken together, our results fill an important knowledge gap concerning the structure and function of the TFLL on the whole.
  • Haslinger, Simone; Hietala, Sami; Hummel, Michael; Maunu, Sirkka Liisa; Sixta, Herbert (2019)
    The valorization of cellulose rich textile waste is promoted by the development of a novel solid-state NMR method for the quantification of cellulose and polyester in textile blends. We applied C-13 CP-MAS NMR as a tool for the quantification and structural characterization of cellulose in cotton polyester blends. Gaussian functions were used to integrate the spectra obtained from a set of calibration standards in order to calculate a sigmoidal calibration curve. Acid hydrolysis was chosen as a reference method. The results demonstrated that solid-state NMR enables a reliable determination of cellulose and polyester in both preconsumer and postconsumer waste textiles and suggests a possible extension of the concept to blends of man-made cellulose fibers (MMCFs) and polyester.
  • Edlund, Petra; Takala, Heikki; Claesson, Elin; Henry, Leocadie; Dods, Robert; Lehtivuori, Heli; Panman, Matthijs; Pande, Kanupriya; White, Thomas; Nakane, Takanori; Berntsson, Oskar; Gustavsson, Emil; Bath, Petra; Modi, Vaibhav; Roy-Chowdhury, Shatabdi; Zook, James; Berntsen, Peter; Pandey, Suraj; Poudyal, Ishwor; Tenboer, Jason; Kupitz, Christopher; Barty, Anton; Fromme, Petra; Koralek, Jake D.; Tanaka, Tomoyuki; Spence, John; Liang, Mengning; Hunter, Mark S.; Boutet, Sebastien; Nango, Eriko; Moffat, Keith; Groenhof, Gerrit; Ihalainen, Janne; Stojkovic, Emina A.; Schmidt, Marius; Westenhoff, Sebastian (2016)
    Phytochromes are a family of photoreceptors that control light responses of plants, fungi and bacteria. A sequence of structural changes, which is not yet fully understood, leads to activation of an output domain. Time-resolved serial femtosecond crystallography (SFX) can potentially shine light on these conformational changes. Here we report the room temperature crystal structure of the chromophore-binding domains of the Deinococcus radiodurans phytochrome at 2.1 angstrom resolution. The structure was obtained by serial femtosecond X-ray crystallography from microcrystals at an X-ray free electron laser. We find overall good agreement compared to a crystal structure at 1.35 angstrom resolution derived from conventional crystallography at cryogenic temperatures, which we also report here. The thioether linkage between chromophore and protein is subject to positional ambiguity at the synchrotron, but is fully resolved with SFX. The study paves the way for time-resolved structural investigations of the phytochrome photocycle with time-resolved SFX.
  • Cellini, Andrea; Wahlgren, Weixiao Yuan; Henry, Leocadie; Pandey, Suraj; Ghosh, Swagatha; Castillon, Leticia; Claesson, Elin; Takala, Heikki; Kubel, Joachim; Nimmrich, Amke; Kuznetsova, Valentyna; Nango, Eriko; Iwata, So; Owada, Shigeki; Stojkovic, Emina A.; Schmidt, Marius; Ihalainen, Janne A.; Westenhoff, Sebastian (2021)
    (6-4) photolyases are flavoproteins that belong to the photolyase/cryptochrome family. Their function is to repair DNA lesions using visible light. Here, crystal structures of Drosophila melanogaster (6-4) photolyase [Dm(6-4)photolyase] at room and cryogenic temperatures are reported. The room-temperature structure was solved to 2.27 angstrom resolution and was obtained by serial femtosecond crystallography (SFX) using an X-ray free-electron laser. The crystallization and preparation conditions are also reported. The cryogenic structure was solved to 1.79 angstrom resolution using conventional X-ray crystallography. The structures agree with each other, indicating that the structural information obtained from crystallography at cryogenic temperature also applies at room temperature. Furthermore, UV-Vis absorption spectroscopy confirms that Dm(6-4)photolyase is photoactive in the crystals, giving a green light to time-resolved SFX studies on the protein, which can reveal the structural mechanism of the photoactivated protein in DNA repair.