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Sample records for ostetud dvdst teha

  1. Hydrogen Fluoride and Fluorine Dispersion Models Integration Into the Air Force Dispersion Assessment Model. Volume 1

    DTIC Science & Technology

    1990-12-07

    and other related information. (ix) This page Is left blank Intentionally (x) EXECUTIVE SUMMARY The Air Force Dispersion Assessment Model ("ADAM...been modeled. In the case of mixing of pure vapor, initially diluted with nitrogen vapor a similar themodynamic modeling approach as teha above is used...model were integrated into ADAM. 6. Routines in ADAM related to the determination of atmospheric stability were improved. 7. ADAM was modified to take

  2. Integrating remote sensing and conventional grazing/browsing models for modelling carrying capacity in southern African rangelands

    NASA Astrophysics Data System (ADS)

    Adjorlolo, C.; Botha, J. O.; Mhangara, P.; Mutanga, O.; Odindi, J.

    2014-10-01

    Woody vegetation encroachment into grasslands or bush thickening, a global phenomenon, is transforming the Southern African grassland systems into savanna-like landscapes. Estimation of woody vegetation is important to rangeland scientists and land managers for assessing its impact on grass production and calculating its grazing and browsing capacity. Assessment of grazing and browsing components is often challenging because agro-ecological landscapes of this region are largely characterized by small scale and heterogeneous land-use-land-cover patterns. In this study, we investigated the utility of high spatial resolution remotely sensing data for modelling grazing and browsing capacity at landscape level. Woody tree density or Tree Equivalents (TE) and Total Leaf Mass (LMASS) data were derived using the Biomass Estimation for Canopy Volume (BECVOL) program. The Random Forest (RF) regression algorithm was assessed to establish relationships between these variables and vegetation indices (Simple Ratio and Normalized Difference Vegetation Index), calculated using the red and near infrared bands of SPOT5. The RF analysis predicted LMASS with R2 = 0.63 and a Root Mean Square Error (RMSE) of 1256 kg/ha compared to a mean of 2291kg/ha. TE was predicted with R2 = 0.55 and a RMSE = 1614 TE/ha compared to a mean of 3746 TE/ha. Next, spatial distribution maps of LMASS/ha and TE/ha were derived using separate RF regression models. The resultant maps were then used as input data into conventional grazing and browsing capacity models to calculate grazing and browsing capacity maps for the study area. This study provides a sound platform for integrating currently available and future remote sensing satellite data into rangeland carrying capacity modelling and monitoring.

  3. Structure determination of an integral membrane protein at room temperature from crystals in situ.

    PubMed

    Axford, Danny; Foadi, James; Hu, Nien Jen; Choudhury, Hassanul Ghani; Iwata, So; Beis, Konstantinos; Evans, Gwyndaf; Alguel, Yilmaz

    2015-06-01

    The structure determination of an integral membrane protein using synchrotron X-ray diffraction data collected at room temperature directly in vapour-diffusion crystallization plates (in situ) is demonstrated. Exposing the crystals in situ eliminates manual sample handling and, since it is performed at room temperature, removes the complication of cryoprotection and potential structural anomalies induced by sample cryocooling. Essential to the method is the ability to limit radiation damage by recording a small amount of data per sample from many samples and subsequently assembling the resulting data sets using specialized software. The validity of this procedure is established by the structure determination of Haemophilus influenza TehA at 2.3 Å resolution. The method presented offers an effective protocol for the fast and efficient determination of membrane-protein structures at room temperature using third-generation synchrotron beamlines.

  4. Structure determination of an integral membrane protein at room temperature from crystals in situ

    SciTech Connect

    Axford, Danny; Foadi, James; Hu, Nien-Jen; Choudhury, Hassanul Ghani; Iwata, So; Beis, Konstantinos; Evans, Gwyndaf; Alguel, Yilmaz

    2015-05-14

    The X-ray structure determination of an integral membrane protein using synchrotron diffraction data measured in situ at room temperature is demonstrated. The structure determination of an integral membrane protein using synchrotron X-ray diffraction data collected at room temperature directly in vapour-diffusion crystallization plates (in situ) is demonstrated. Exposing the crystals in situ eliminates manual sample handling and, since it is performed at room temperature, removes the complication of cryoprotection and potential structural anomalies induced by sample cryocooling. Essential to the method is the ability to limit radiation damage by recording a small amount of data per sample from many samples and subsequently assembling the resulting data sets using specialized software. The validity of this procedure is established by the structure determination of Haemophilus influenza TehA at 2.3 Å resolution. The method presented offers an effective protocol for the fast and efficient determination of membrane-protein structures at room temperature using third-generation synchrotron beamlines.