Glenn Research Center Quantum Communicator Receiver Design and Development

We investigate, design, and develop a prototype real-time synchronous receiver for the second-generation quantum communicator recently developed at the National Aeronautics and Space Administration (NASA) Glenn Research Center. This communication system exploits the temporal coincidences between simultaneously fired low-power laser sources to communicate at power levels several orders of magnitude less than what is currently achievable through classical means, with the ultimate goal of creating ultra-low-power microsize optical communications and sensing devices. The proposed receiver uses a unique adaptation of the early-late gate method for symbol synchronization and a newly identified 31-bit synchronization word for frame synchronization. This receiver, implemented in a field-programmable gate array (FPGA), also provides a number of significant additional features over the existing non-real-time experimental receiver, such as real-time bit error rate (BER) statistics collection and display, and recovery and display of embedded textual information. It also exhibits an indefinite run time and statistics collection. (c) 2009 Society of Photo-Optical Instrumentation Engineers

Glenn Research Center Quantum Communicator Receiver Design and Development

We investigate, design, and develop a prototype real-time synchronous receiver for the second-generation quantum communicator recently developed at the National Aeronautics and Space Administration (NASA) Glenn Research Center. This communication system exploits the temporal coincidences between simultaneously fired low-power laser sources to communicate at power levels several orders of magnitude less than what is currently achievable through classical means, with the ultimate goal of creating ultra-low-power microsize optical communications and sensing devices. The proposed receiver uses a unique adaptation of the early-late gate method for symbol synchronization and a newly identified 31-bit synchronization word for frame synchronization. This receiver, implemented in a field-programmable gate array (FPGA), also provides a number of significant additional features over the existing non-real-time experimental receiver, such as real-time bit error rate (BER) statistics collection and display, and recovery and display of embedded textual information. It also exhibits an indefinite run time and statistics collection. (c) 2009 Society of Photo-Optical Instrumentation Engineers

Bodies, technology, and the edgework of urban exploration

We have determined the structure of the archaeal sodium/proton antiporter NhaP1 at 7 Å resolution by electron crystallography of 2D crystals. NhaP1 is a dimer in the membrane, with 13 membrane-spanning α-helices per protomer, whereas the distantly related bacterial NhaA has 12. Dimer contacts in the two antiporters are very different, but the structure of a six-helix bundle at the tip of the protomer is conserved. The six-helix bundle of NhaA contains two partially unwound α-helices thought to harbour the ion-translocation site, which is thus similar in NhaP1. A model of NhaP1 based on detailed sequence comparison and the NhaA structure was fitted to the 7 Å map. The additional N-terminal helix 1 of NhaP1, which appears to be an uncleaved signal sequence, is located near the dimer interface. Similar sequences are present in many eukaryotic homologues of NhaP1, including NHE1. Although fully folded and able to dimerize, NhaP1 constructs without helix 1 are inactive. Possible reasons are investigated and discussed

A structural model for monastrol inhibition of dimeric kinesin Eg5

Eg5 or KSP is a homotetrameric Kinesin-5 involved in centrosome separation and assembly of the bipolar mitotic spindle. Analytical gel filtration of purified protein and cryo-electron microscopy (cryo-EM) of unidirectional shadowed microtubule–Eg5 complexes have been used to identify the stable dimer Eg5-513. The motility assays show that Eg5-513 promotes robust plus-end-directed microtubule gliding at a rate similar to that of homotetrameric Eg5 in vitro. Eg5-513 exhibits slow ATP turnover, high affinity for ATP, and a weakened affinity for microtubules when compared to monomeric Eg5. We show here that the Eg5-513 dimer binds microtubules with both heads to two adjacent tubulin heterodimers along the same microtubule protofilament. Under all nucleotide conditions tested, there were no visible structural changes in the monomeric Eg5–microtubule complexes with monastrol treatment. In contrast, there was a substantial monastrol effect on dimeric Eg5-513, which reduced microtubule lattice decoration. Comparisons between the X-ray structures of Eg5-ADP and Eg5-ADP-monastrol with rat kinesin-ADP after docking them into cryo-EM 3-D scaffolds revealed structural evidence for the weaker microtubule–Eg5 interaction in the presence of monastrol