161 research outputs found
Universal Microwave Photonics Approach to Frequency-Coded Quantum Key Distribution
Design principles of universal microwave photonics system (MPS) for quantum key distribution (QKD) with frequency coding are concerned. Its main modulation concept lies in single photon generation on sidebands of optical carrier and determination of photons ground state through its registration and the amplitude value of its carrier frequency as reference channel. So, it is necessary to solve problems of signal-to-carrier ratio of single photon detector (SPD) and aspects of photon number splitting (PNS) attack, nonlinear phase modulation (NPM) between carrier and sidebands in fiber, and finally, spectral selection of carrier in receiver. The technologies, based on the modulation conversion of an optical carrier, are widely used in microwave photonics. Due to the natural symmetry of modulated signals and the highest achievable ratio of the modulation conversions, amplitude-phase modulation with complete or partial suppression of the optical carrier has found a particularly wide application in MPS. The characteristics of advanced MPS for QKD with frequency coding and carrier suppression based on tandem amplitude modulation and phase commutation are presented. New systems can have classical symmetric or non-classical asymmetric structure for QKD based only on spectral selection of carrier and subcarriers without re-modulation
Influence of parameters of delayed asphalt coking process on yield and quality of liquid and solid-phase products
Paper studies the effect of excess pressure during delayed coking of asphalt, obtained by propane deasphaltization of tar, on yield and physical and chemical properties of hydrocarbon fuels' components and solid-phase product – petroleum coke. Asphalt was coked at a temperature of 500 °C and excess pressure of 0.15-0.35 MPa in a laboratory unit for delayed coking of periodic action. Physical and chemical properties of raw materials and components of light (gasoline), medium (light gasoil), and heavy (heavy gasoil) distillates obtained during experimental study were determined: density, viscosity, coking ability, sulfur content, iodine number, pour points, flash points, fluidity loss and fractional composition. Quantitative group hydrocarbon and microelement compositions and properties of obtained samples of petroleum coke (humidity, ash content, volatiles' yield, sulfur content, etc.) were also studied. Comparative assessment of their quality is given in accordance with requirements of GOST 22898-78 “Low-sulfur petroleum coke. Specifications”. In addition, patterns of changes in excess coking pressure on yield and quality indicators of distillate products and petroleum coke were revealed. With an increase in excess pressure of coking process from 0.15 to 0.35 MPa, content of paraffin-naphthenic hydrocarbons in light and heavy gasoils of delayed coking decreases. Common pattern in asphalt coking is an increase in yield of coke and hydrocarbon gas with an increase in excess pressure from 0.15 to 0.35 MPa
Mechanism of ribosome shutdown by RsfS in Staphylococcus aureus revealed by integrative structural biology approach.
Funder: The Russian Government Program of Competitive Growth of Kazan Federal UniversityFor the sake of energy preservation, bacteria, upon transition to stationary phase, tone down their protein synthesis. This process is favored by the reversible binding of small stress-induced proteins to the ribosome to prevent unnecessary translation. One example is the conserved bacterial ribosome silencing factor (RsfS) that binds to uL14 protein onto the large ribosomal subunit and prevents its association with the small subunit. Here we describe the binding mode of Staphylococcus aureus RsfS to the large ribosomal subunit and present a 3.2 Å resolution cryo-EM reconstruction of the 50S-RsfS complex together with the crystal structure of uL14-RsfS complex solved at 2.3 Å resolution. The understanding of the detailed landscape of RsfS-uL14 interactions within the ribosome shed light on the mechanism of ribosome shutdown in the human pathogen S. aureus and might deliver a novel target for pharmacological drug development and treatment of bacterial infections
Structural basis of ABCF-mediated resistance to pleuromutilin, lincosamide, and streptogramin A antibiotics in Gram-positive pathogens
he antibiotic target. One class of such proteins are the antibiotic resistance (ARE) ATP-binding cassette (ABC) proteins of the F-subtype (ARE-ABCFs), which are widely distributed throughout Gram-positive bacteria and bind the ribosome to alleviate translational inhibition from antibiotics that target the large ribosomal subunit. Here, we present single-particle cryo-EM structures of ARE-ABCF-ribosome complexes from three Gram-positive pathogens: Enterococcus faecalis LsaA, Staphylococcus haemolyticus VgaALC and Listeria monocytogenes VgaL. Supported by extensive mutagenesis analysis, these structures enable a general model for antibiotic resistance mediated by these ARE-ABCFs to be proposed. In this model, ABCF binding to the antibiotic-stalled ribosome mediates antibiotic release via mechanistically diverse long-range conformational relays that converge on a few conserved ribosomal RNA nucleotides located at the peptidyltransferase center. These insights are important for the future development of antibiotics that overcome such target protection resistance mechanisms
The re-refined crystal structure of the Haloarcula marismortui large ribosomal subunit at 2.4 Angstrom resolution: more complete structure of the L7/L12 and L1 stalk, L5 and LX proteins. This entry contains LX protein and water molecules.
The re-refined crystal structure of the Haloarcula marismortui large ribosomal subunit at 2.4 Angstrom resolution: more complete structure of the L7/L12 and L1 stalk, L5 and LX proteins
The re-refined crystal structure of the Haloarcula marismortui large ribosomal subunit at 2.4 Angstrom resolution: more complete structure of the L7/L12 and L1 stalk, L5 and LX proteins
The re-refined crystal structure of the Haloarcula marismortui large ribosomal subunit at 2.4 Angstrom resolution: more complete structure of the L7/L12 and L1 stalk, L5 and LX proteins
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