Quenched Narrow-Line Laser Cooling of 40Ca to Near the Photon Recoil Limit

We present a cooling method that should be generally applicable to atoms with narrow optical transitions. This technique uses velocity-selective pulses to drive atoms towards a zero-velocity dark state and then quenches the excited state to increase the cooling rate. We demonstrate this technique of quenched narrow-line cooling by reducing the 1-D temperature of a sample of neutral 40Ca atoms. We velocity select and cool with the 1S0(4s2) to 3P1(4s4p) 657 nm intercombination line and quench with the 3P1(4s4p) to 1S0(4s5s) intercombination line at 553 nm, which increases the cooling rate eight-fold. Limited only by available quenching laser power, we have transferred 18 % of the atoms from our initial 2 mK velocity distribution and achieved temperatures as low as 4 microK, corresponding to a vrms of 2.8 cm/s or 2 recoils at 657 nm. This cooling technique, which is closely related to Raman cooling, can be extended to three dimensions.Comment: 5 pages, 4 figures; Submitted to PRA Rapid Communication

Autonomous gauge for blast impulse determination close to explosive charges

This paper reports on a new gauge for blast impulse determination close to explosive charges. The gauge is based on the autonomous data recorder g-rec developed at the Ernst-Mach-Institute for data acquisition in harsh environments. Combined with an acceleration sensor these data recorders allow for the direct determination of the momentum transferred to an object by a blast wave even in the immediate vicinity of the explosive charge. From this the blast impulse can be determined. Using autonomous electronics distinct advantages are gained compared to classical passive momentum traps. The paper summarizes the properties of the g-rec recorder and describes the setup of the autonomous momentum trap in detail. Numerical simulations are presented which illustrate the gauge performance and its limitations. Tests with 1 kg charges demonstrate the feasibility of the approach. Good agreement was found between simulations and tests. The application range of the gauges is determined by the measurement range of the built-in acceleration sensor and its overall dimensions and weight. The present configuration is designed for distances between ∼0.3 and 1 m from charges between several 100 g and several kilograms. Data were successfully collected down to reduced distances of 0.25 m/kg1/3. Minor changes in gauge dimensions, weight, or measurement range enable the gauges to be deployed at even closer distances

Interferometrie mit laserpraeparierten Kalziumatomen zur Realisierung eines Frequenznormals

By investigations of Ramsey resonances at laser cooled Ca atoms it is demonstrated that with cool atom beams frequency standards are available with instabilities about 10 "-"1"4 ( "s"/ t_M) "1"/"2 and uncertainties #partial deriv##nu#/#nu# #approx# 10 "-"1"4 . The uncertainty can be reduced to < 10 "-"1"5 using pulsed excitements and laser trapped atoms. The frequency standard can be further improved by back-pumping of the "1D_2 state population via 5"1P_1 state into the cooling cycle and using the intercombination line for the cooling process. (WEN)SIGLEAvailable from TIB Hannover: RA 3254(40) / FIZ - Fachinformationszzentrum Karlsruhe / TIB - Technische InformationsbibliothekDEGerman

Oma1, a novel membrane-bound metallopeptidase in mitochondria with activities overlapping with the m-AAA protease

The integrity of the inner membrane of mitochondria is maintained by a membrane-embedded quality control system that ensures the removal of misfolded membrane proteins. Two ATP-dependent AAA proteases with catalytic sites at opposite membrane surfaces are key components of this proteolytic system. Here we describe the identification of a novel conserved metallopeptidase that exerts activities overlapping with the m-AAA protease and was therefore termed Oma1. Both peptidases are integral parts of the inner membrane and mediate the proteolytic breakdown of a misfolded derivative of the polytopic inner membrane protein Oxa1. The m-AAA protease cleaves off the matrix-exposed C-terminal domain of Oxa1 and processively degrades its transmembrane domain. In the absence of the m-AAA protease, proteolysis of Oxa1 is mediated in an ATP-independent manner by Oma1 and a yet unknown peptidase resulting in the accumulation of N- and C-terminal proteolytic fragments. Oma1 exposes its proteolytic center to the matrix side; however, mapping of Oma1 cleavage sites reveals clipping of Oxa1 in loop regions at both membrane surfaces. These results identify Oma1 as a novel component of the quality control system in the inner membrane of mitochondria. Proteins homologous to Oma1 are present in higher eukaryotic cells, eubacteria and archaebacteria, suggesting that Oma1 is the founding member of a conserved family of membrane-embedded metallopeptidases