MOSFIRE, the multi-object spectrometer for infra-red exploration at the Keck Observatory

This paper describes the as-built performance of MOSFIRE, the multi-object spectrometer and imager for the Cassegrain focus of the 10-m Keck 1 telescope. MOSFIRE provides near-infrared (0.97 to 2.41 μm) multi-object spectroscopy over a 6.1' x 6.1' field of view with a resolving power of R~3,500 for a 0.7" (0.508 mm) slit (2.9 pixels in the dispersion direction), or imaging over a field of view of ~6.9' diameter with ~0.18" per pixel sampling. A single diffraction grating can be set at two fixed angles, and order-sorting filters provide spectra that cover the K, H, J or Y bands by selecting 3rd, 4th, 5th or 6th order respectively. A folding flat following the field lens is equipped with piezo transducers to provide tip/tilt control for flexure compensation at the <0.1 pixel level. Instead of fabricated focal plane masks requiring frequent cryo-cycling of the instrument, MOSFIRE is equipped with a cryogenic Configurable Slit Unit (CSU) developed in collaboration with the Swiss Center for Electronics and Microtechnology (CSEM). Under remote control the CSU can form masks containing up to 46 slits with ~0.007-0.014" precision. Reconfiguration time is < 6 minutes. Slits are formed by moving opposable bars from both sides of the focal plane. An individual slit has a length of 7.0" but bar positions can be aligned to make longer slits in increments of 7.5". When masking bars are retracted from the field of view and the grating is changed to a mirror, MOSFIRE becomes a wide-field imager. The detector is a 2K x 2K H2-RG HgCdTe array from Teledyne Imaging Sensors with low dark current and low noise. Results from integration and commissioning are presented

MOSFIRE, the multi-object spectrometer for infra-red exploration at the Keck Observatory

This paper describes the as-built performance of MOSFIRE, the multi-object spectrometer and imager for the Cassegrain focus of the 10-m Keck 1 telescope. MOSFIRE provides near-infrared (0.97 to 2.41 μm) multi-object spectroscopy over a 6.1' x 6.1' field of view with a resolving power of R~3,500 for a 0.7" (0.508 mm) slit (2.9 pixels in the dispersion direction), or imaging over a field of view of ~6.9' diameter with ~0.18" per pixel sampling. A single diffraction grating can be set at two fixed angles, and order-sorting filters provide spectra that cover the K, H, J or Y bands by selecting 3rd, 4th, 5th or 6th order respectively. A folding flat following the field lens is equipped with piezo transducers to provide tip/tilt control for flexure compensation at the <0.1 pixel level. Instead of fabricated focal plane masks requiring frequent cryo-cycling of the instrument, MOSFIRE is equipped with a cryogenic Configurable Slit Unit (CSU) developed in collaboration with the Swiss Center for Electronics and Microtechnology (CSEM). Under remote control the CSU can form masks containing up to 46 slits with ~0.007-0.014" precision. Reconfiguration time is < 6 minutes. Slits are formed by moving opposable bars from both sides of the focal plane. An individual slit has a length of 7.0" but bar positions can be aligned to make longer slits in increments of 7.5". When masking bars are retracted from the field of view and the grating is changed to a mirror, MOSFIRE becomes a wide-field imager. The detector is a 2K x 2K H2-RG HgCdTe array from Teledyne Imaging Sensors with low dark current and low noise. Results from integration and commissioning are presented

Electrochemical and Photoelectrochemical Investigation of Water Oxidation with Hematite Electrodes

Atomic layer deposition (ALD) was utilized to deposit uniform thin films of hematite (α-Fe2O3) on transparent conductive substrates for photocatalytic water oxidation studies. Comparison of the oxidation of water to the oxidation of a fast redox shuttle allowed for new insight in determining the rate limiting processes of water oxidation at hematite electrodes. It was found that an additional overpotential is needed to initiate water oxidation compared to the fast redox shuttle. A combination of electrochemical impedance spectroscopy, photoelectrochemical and electrochemical measurements were employed to determine the cause of the additional overpotential. It was found that photogenerated holes initially oxidize the electrode surface under water oxidation conditions, which is attributed to the first step in water oxidation. A critical number of these surface intermediates need to be generated in order for the subsequent hole-transfer steps to proceed. At higher applied potentials, the behavior of the electrode is virtually identical while oxidizing either water or the fast redox shuttle; the slight discrepancy is attributed to a shift in potential associated with Fermi level pinning by the surface states in the absence of a redox shuttle. A water oxidation mechanism is proposed to interpret these results

Regulated Expression of the Escherichia coli lepB Gene as a Tool for Cellular Testing of Antimicrobial Compounds That Inhibit Signal Peptidase I In Vitro

Escherichia coli under-expressing lepB was utilized to test cellular inhibition of signal peptidase I (SPase). For the construction of a lepB regulatable strain, the E. coli lepB gene was cloned into pBAD, with expression dependent on l-arabinose. The chromosomal copy of lepB was replaced with a kanamycin resistance gene, which was subsequently removed. SPase production by the lepB regulatable strain in the presence of various concentrations of l-arabinose was monitored by Western blot analysis. At lower arabinose concentrations growth proceeded more slowly, possibly due to a decrease of SPase levels in the cells. A penem SPase inhibitor with little antimicrobial activity against E. coli when tested at 100 μM was utilized to validate the cell-based system. Under-expression of lepB sensitized the cells to penem, with complete growth inhibition observed at 10 to 30 μM. Growth was rescued by increasing the SPase levels. The cell-based assay was used to test cellular inhibition of SPase by compounds that inhibit the enzyme in vitro. MD1, MD2, and MD3 are SPase inhibitors with antimicrobial activity against Staphylococcus aureus, although they do not inhibit growth of E. coli. MD1 presented the best spectrum of antimicrobial activity. Both MD1 and MD2 prevented growth of E. coli under-expressing lepB in the presence of polymyxin B nonapeptide, with growth rescue observed when wild-type levels of SPase were produced. MD3 and MD4, a reactive analog of MD3, inhibited growth of E. coli under-expressing lepB. However, growth rescue in the presence of these compounds following increased lepB expression was observed only after prolonged incubation