Fabrication, structure, and electron emission of single carbon nanotubes

Carbon nanotubes possess many excellent field emission properties. An obstacle to these applications is that there is no simple and reproducible method to prepare a single carbon nanotube field emitter. In this dissertation, individual carbon nanotube field emitters have been fabricated in a two-step process involving (a) producing micron-size carbon fibers which contain single carbon nanotubes at their cores and (b) exposing the nanotubes by fracturing the fiber with mechanical forces and mounting the fiber to a copper ribbon with a groove. This fabrication method has the potential to be the production method for single carbon nanotube field emission point electron sources. The cold field emission properties of single carbon nanotubes have been studied. These carbon nanotubes exhibit large field enhancement factors of 1.1×107 m-1 and low turn-on fields of 1.1 V/?m. An empirical model has been developed to calculate the field enhancement factor of an open end nanotube attached on a carbon fiber. The lifetime measurements show that a single carbon nanotube can continuously emit electrons over 100 hours without significant current drops. The emission stability measurements show that the maximum current drift is 3.6%. It is also shown experimentally that a carbon nanotube has a high reduced brightness 2.9×108 ASr-1m-2V-1, which is two orders of magnitude higher than those of the thermionic electron sources. The thermal field emission properties of a single carbon nanotube have been systemically studied. It is found that there is a gap between the intermediate region and the field emission region which is not covered by either the Fowler-Nordheim theory or the Murphy-Good theory. We have developed an analytical equation that describes the thermal field emission behavior of a single carbon nanotube within the gap. The experimental results agree well with the theoretical predictions. We also studied the effect of Cs doping on the field emission properties and electronic properties of a single nanotube. We found that the work function of the carbon nanotube was reduced from 4.8 eV to 3.7 eV by Cs doping

Channel Estimation for Ambient Backscatter Communication Systems with Massive-Antenna Reader

Ambient backscatter, an emerging green communication technology, has aroused great interest from both academia and industry. One open problem for ambient backscatter communication (AmBC) systems is channel estimation for a massive-antenna reader. In this paper, we focus on channel estimation problem in AmBC systems with uniform linear array (ULA) at the reader which consists of large number of antennas. We first design a two-step method to jointly estimate channel gains and direction of arrivals (DoAs), and then refine the estimates through angular rotation. Additionally, Cramer-Rao lower bounds (CRLBs) are derived for both the modulus of the channel gain and the DoA estimates. Simulations are then provided to validate the analysis, and to show the efficiency of the proposed approach.Comment: 5 figures, submitted to IEEE Transactions on Vehicular Technology, 29 March, 201

Structure of HIV-1 Capsid Assemblies by Cryo-electron Microscopy and Iterative Helical Real-space Reconstruction

Cryo-electron microscopy (cryo-EM), combined with image processing, is an increasingly powerful tool for structure determination of macromolecular protein complexes and assemblies. In fact, single particle electron microscopy1 and two-dimensional (2D) electron crystallography2 have become relatively routine methodologies and a large number of structures have been solved using these methods. At the same time, image processing and three-dimensional (3D) reconstruction of helical objects has rapidly developed, especially, the iterative helical real-space reconstruction (IHRSR) method3, which uses single particle analysis tools in conjunction with helical symmetry. Many biological entities function in filamentous or helical forms, including actin filaments4, microtubules5, amyloid fibers6, tobacco mosaic viruses7, and bacteria flagella8, and, because a 3D density map of a helical entity can be attained from a single projection image, compared to the many images required for 3D reconstruction of a non-helical object, with the IHRSR method, structural analysis of such flexible and disordered helical assemblies is now attainable

Structure and dynamics of the E. coli chemotaxis core signaling complex by cryo-electron tomography and molecular simulations

To enable the processing of chemical gradients, chemotactic bacteria possess large arrays of transmembrane chemoreceptors, the histidine kinase CheA, and the adaptor protein CheW, organized as coupled core-signaling units (CSU). Despite decades of study, important questions surrounding the molecular mechanisms of sensory signal transduction remain unresolved, owing especially to the lack of a high-resolution CSU structure. Here, we use cryo-electron tomography and sub-tomogram averaging to determine a structure of the Escherichia coli CSU at sub-nanometer resolution. Based on our experimental data, we use molecular simulations to construct an atomistic model of the CSU, enabling a detailed characterization of CheA conformational dynamics in its native structural context. We identify multiple, distinct conformations of the critical P4 domain as well as asymmetries in the localization of the P3 bundle, offering several novel insights into the CheA signaling mechanism

Protease Cleavage Leads to Formation of Mature Trimer Interface in HIV-1 Capsid

During retrovirus particle maturation, the assembled Gag polyprotein is cleaved by the viral protease into matrix (MA), capsid (CA), and nucleocapsid (NC) proteins. To form the mature viral capsid, CA rearranges, resulting in a lattice composed of hexameric and pentameric CA units. Recent structural studies of assembled HIV-1 CA revealed several inter-subunit interfaces in the capsid lattice, including a three-fold interhexamer interface that is critical for proper capsid stability. Although a general architecture of immature particles has been provided by cryo-electron tomographic studies, the structural details of the immature particle and the maturation pathway remain unknown. Here, we used cryo-electron microscopy (cryoEM) to determine the structure of tubular assemblies of the HIV-1 CA-SP1-NC protein. Relative to the mature assembled CA structure, we observed a marked conformational difference in the position of the CA-CTD relative to the NTD in the CA-SP1-NC assembly, involving the flexible hinge connecting the two domains. This difference was verified via engineered disulfide crosslinking, revealing that inter-hexamer contacts, in particular those at the pseudo three-fold axis, are altered in the CA-SP1-NC assemblies compared to the CA assemblies. Results from crosslinking analyses of mature and immature HIV-1 particles containing the same Cys substitutions in the Gag protein are consistent with these findings. We further show that cleavage of preassembled CA-SP1-NC by HIV-1 protease in vitro leads to release of SP1 and NC without disassembly of the lattice. Collectively, our results indicate that the proteolytic cleavage of Gag leads to a structural reorganization of the polypeptide and creates the three-fold interhexamer interface, important for the formation of infectious HIV-1 particles. © 2012 Meng et al

Fabrication and characterization of single carbon nanotube emitters as point electron sources

Individual carbon nanotube electron field emitters with good controllability have been fabricated in a two-step process involving (a) producing micron-size carbon fibers which contain single carbon nanotubes at their cores by a chemical vapor deposition method and (b) exposing the nanotubes by fracturing the fiber with mechanical forces and mounting the fiber to a copper wire. These fiber-nanotube electron emitters show low operating voltage, generate high field enhancement, and produce fine electron beams. The field emission characteristics and durability of this structure offer promising applications for analytical instruments where high performance point electron sources are required

Field emission of electrons from a Cs-doped single carbon nanotube of known chiral indices

The authors report the effects of Cs doping on the field emission properties of a five-shell single carbon nanotube. The chiral indices of each shell of this carbon nanotube have been determined using nanobeam electron diffraction, which has four semiconducting shells and one metallic shell in the middle. From the Fowler-Nordheim plots, a reduction from 4.8 to 3.8 eV has been observed in the work function of the single carbon nanotube before and after Cs doping

Rhesus TRIM5α disrupts the HIV-1 capsid at the inter-hexamer interfaces

TRIM proteins play important roles in the innate immune defense against retroviral infection, including human immunodeficiency virus type-1 (HIV-1). Rhesus macaque TRIM5α (TRIM5αrh) targets the HIV-1 capsid and blocks infection at an early post-entry stage, prior to reverse transcription. Studies have shown that binding of TRIM5α to the assembled capsid is essential for restriction and requires the coiled-coil and B30.2/SPRY domains, but the molecular mechanism of restriction is not fully understood. In this study, we investigated, by cryoEM combined with mutagenesis and chemical cross-linking, the direct interactions between HIV-1 capsid protein (CA) assemblies and purified TRIM5αrh containing coiled-coil and SPRY domains (CC-SPRYrh). Concentration-dependent binding of CC-SPRYrh to CA assemblies was observed, while under equivalent conditions the human protein did not bind. Importantly, CC-SPRYrh, but not its human counterpart, disrupted CA tubes in a non-random fashion, releasing fragments of protofilaments consisting of CA hexamers without dissociation into monomers. Furthermore, such structural destruction was prevented by inter-hexamer crosslinking using P207C/T216C mutant CA with disulfide bonds at the CTD-CTD trimer interface of capsid assemblies, but not by intra-hexamer crosslinking via A14C/E45C at the NTD-NTD interface. The same disruption effect by TRIM5αrh on the inter-hexamer interfaces also occurred with purified intact HIV-1 cores. These results provide insights concerning how TRIM5α disrupts the virion core and demonstrate that structural damage of the viral capsid by TRIM5α is likely one of the important components of the mechanism of TRIM5α-mediated HIV-1 restriction. © 2011 Zhao et al

Mature Hiv-1 Capsid Structure By Cryo-Electron Microscopy And All-Atom Molecular Dynamics

Retroviral capsid proteins are conserved structurally but assemble into different morphologies. The mature human immunodeficiency virus-1 (HIV-1) capsid is best described by a \u27fullerene cone\u27 model, in which hexamers of the capsid protein are linked to form a hexagonal surface lattice that is closed by incorporating 12 capsid-protein pentamers. HIV-1 capsid protein contains an amino-terminal domain (NTD) comprising seven α-helices and a β-hairpin, a carboxy-terminal domain (CTD) comprising four α-helices, and a flexible linker with a 3 10-helix connecting the two structural domains. Structures of the capsid-protein assembly units have been determined by X-ray crystallography; however, structural information regarding the assembled capsid and the contacts between the assembly units is incomplete. Here we report the cryo-electron microscopy structure of a tubular HIV-1 capsid-protein assembly at 8 Å resolution and the three-dimensional structure of a native HIV-1 core by cryo-electron tomography. The structure of the tubular assembly shows, at the three-fold interface, a three-helix bundle with critical hydrophobic interactions. Mutagenesis studies confirm that hydrophobic residues in the centre of the three-helix bundle are crucial for capsid assembly and stability, and for viral infectivity. The cryo-electron-microscopy structures enable modelling by large-scale molecular dynamics simulation, resulting in all-atom models for the hexamer-of-hexamer and pentamer-of-hexamer elements as well as for the entire capsid. Incorporation of pentamers results in closer trimer contacts and induces acute surface curvature. The complete atomic HIV-1 capsid model provides a platform for further studies of capsid function and for targeted pharmacological intervention. © 2013 Macmillan Publishers Limited. All rights reserved