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NASA NTRS2006

Nadir Measurements of Carbon Monoxide Distributions by the Tropospheric Emission Spectrometer Instrument Onboard the Aura Spacecraft: Overview of Analysis Approach and Examples of Initial Results

We provide an overview of the nadir measurements of carbon monoxide (CO) obtained thus far by the Tropospheric Emission Spectrometer (TES). The instrument is a high resolution array Fourier transform spectrometer designed to measure infrared spectral radiances from low Earth orbit. It is one of four instruments successfully launched onboard the Aura platform into a sun synchronous orbit at an altitude of 705 km on July 15, 2004 from Vandenberg Air Force Base, California. Nadir spectra are recorded at 0.06/cm spectral resolution with a nadir footprint of 5 x 8 km. We describe the TES retrieval approach for the analysis of the nadir measurements, report averaging kernels for typical tropical and polar ocean locations, characterize random and systematic errors for those locations, and describe instrument performance changes in the CO spectral region as a function of time. Sample maps of retrieved CO for the middle and upper troposphere from global surveys during December 2005 and April 2006 highlight the potential of the results for measurement and tracking of global pollution and determining air quality from space.

carbon monoxide↗

NASA NTRS2000

Crystallized N-terminal domain of influenza virus matrix protein M1 and method of determining and using same

The matrix protein, M1, of influenza virus strain A/PR/8/34 has been purified from virions and crystallized. The crystals consist of a stable fragment (18 Kd) of the M1 protein. X-ray diffraction studies indicated that the crystals have a space group of P3.sub.t 21 or P3.sub.2 21. Vm calculations showed that there are two monomers in an asymmetric unit. A crystallized N-terminal domain of M1, wherein the N-terminal domain of M1 is crystallized such that the three dimensional structure of the crystallized N-terminal domain of M1 can be determined to a resolution of about 2.1 .ANG. or better, and wherein the three dimensional structure of the uncrystallized N-terminal domain of M1 cannot be determined to a resolution of about 2.1 .ANG. or better. A method of purifying M1 and a method of crystallizing M1. A method of using the three-dimensional crystal structure of M1 to screen for antiviral, influenza virus treating or preventing compounds. A method of using the three-dimensional crystal structure of M1 to screen for improved binding to or inhibition of influenza virus M1. The use of the three-dimensional crystal structure of the M1 protein of influenza virus in the manufacture of an inhibitor of influenza virus M1. The use of the three-dimensional crystal structure of the M1 protein of influenza virus in the screening of candidates for inhibition of influenza virus M1.

Luo, Ming↗