3 research outputs found
Software for the derivation of scaled surface reflectances from AVIRIS data
An operational software program is now available for deriving 'scaled surface reflectances' from spectral data collected by the Airborne Visible/Infrared Imaging Spectrometer (AVIRIS). The program simulates both the atmospheric scattering and absorption effects. Brief descriptions of the algorithm, inputs, outputs, the limitations of the software, and procedures for obtaining the software are given
High Accuracy In-Flight Wavelength Calibration of Imaging Spectrometry Data
Accurate wavelength calibration of imaging spectrometer data is essential if proper atmospheric transmission corrections are to be made to obtain apparent surface reflectance. Accuracies of 0.1 nm are necessary for a 10 nm-sampling instrument in order to match the slopes of the deep atmospheric water vapor features that dominate the 0.7-2.3 micrometer regions. The Airborne Visible/Infrared Imaging Spectrometer (AVIRIS) is calibrated in the laboratory to determine the wavelength position and full-width-half-maximum (FWHM) response for each of the 224 channels. The accuracies are limited by the quality of the monochromator used as a source. The accuracies vary from plus or minus to plus or minus 1.5 nm depending on the wavelength region, in general decreasing with increasing wavelength. Green et al. make corrections to the wavelength calibrations by using the known positions of 14 atmospheric absorption features throughout the 0.4-2.5 micrometer wavelength region. These features, having varying width and intensity, were matched to the MODTRAN model with a non-linear least squares fitting algorithm. A complete calibration was developed for all 224 channels by interpolation. Instrument calibration cannot be assumed to be stable to 0.1 nm over a flight season given the rigors of thermal cycling and launch and landing loads. The upcoming sensor HYDICE will require a means for in-flight spectral calibration of each scene because the calibration is both temperature and pressure sensitive. In addition, any sensor using a two-dimensional array has the potential for systematic wavelength shifts as a function of cross-track position, commonly called 'smile'. Therefore, a rapid means for calibrating complete images will be required. The following describes a method for determining instrument wavelength calibration using atmospheric absorption features that is efficient enough to be used for entire images on workstations. This study shows the effect of the surface reflectance on the calibration accuracy and the calibration history for the AVIRIS B spectrometer over the 1992 flight season
Recommended from our members
Harnessing evolutionary fitness in Plasmodium falciparum for drug discovery and suppressing resistance
Drug resistance emerges in an ecological context where fitness costs restrict the diversity of escape pathways. These pathways are targets for drug discovery, and here we demonstrate that we can identify small-molecule inhibitors that differentially target resistant parasites. Combining wild-type and mutant-type inhibitors may prevent the emergence of competitively viable resistance. We tested this hypothesis with a clinically derived chloroquine-resistant (CQr) malaria parasite and with parasites derived by in vitro selection with Plasmodium falciparum dihydroorotate dehydrogenase (PfDHODH) inhibitors. We screened a chemical library against CQs and CQr lines and discovered a drug-like compound (IDI-3783) that was potent only in the CQr line. Surprisingly, in vitro selection of Plasmodium falciparum resistant to IDI-3783 restored CQ sensitivity, thereby indicating that CQ might once again be useful as a malaria therapy. In parallel experiments, we selected P. falciparum lines resistant to structurally unrelated PfDHODH inhibitors (Genz-666136 and DSM74). Both selections yielded resistant lines with the same point mutation in PfDHODH:E182D. We discovered a compound (IDI-6273) more potent against E182D than wild-type parasites. Selection of the E182D mutant with IDI-6273 yielded a reversion to the wild-type protein sequence and phenotype although the nucleotide sequence was different. Importantly, selection with a combination of Genz-669178, a wild-type PfDHODH inhibitor, and IDI-6273, a mutant-selective PfDHODH inhibitor, did not yield resistant parasites. These two examples demonstrate that the compromise between resistance and evolutionary fitness can be exploited to design therapies that prevent the emergence and spread of resistant organisms.Organismic and Evolutionary Biolog