scholarly journals Ultralow power trapping and fluorescence detection of single particles on an optofluidic chip

Lab on a Chip ◽  
2010 ◽  
Vol 10 (2) ◽  
pp. 189-194 ◽  
Author(s):  
S. Kühn ◽  
B. S. Phillips ◽  
E. J. Lunt ◽  
A. R. Hawkins ◽  
H. Schmidt
Keyword(s):  
Fluorescence Detection ◽  
Single Particles ◽  
Ultralow Power ◽  
Optofluidic Chip

Electro-Optical Detection of Single Nanoparticles on a Nanopore-Optofluidic Chip

2014 ◽  
Vol 1720 ◽  
Author(s):  
Shuo Liu ◽  
Yue Zhao ◽  
Matthew Stott ◽  
Joshua W. Parks ◽  
Aaron R. Hawkins ◽  
...  
Keyword(s):  
Solid State ◽  
Flow Velocity ◽  
Optical Waveguide ◽  
Wavelength Range ◽  
Fluorescence Detection ◽  
Optical Detection ◽  
Liquid Core ◽  
Optical Signals ◽  
Different Types ◽  
Optofluidic Chip

ABSTRACTA solid-state nanopore was integrated into an optofluidic sensor chip, liquid-core anti-resonant reflecting optical waveguide (ARROW). The solid-state nanopore worked as a smart gate, which simultaneously provided characteristic electrical signals and controlled the entry of single nanoparticles into the liquid-core channel. The subsequent fluorescence detection further identified the nanoparticles by providing optical signals within a specific wavelength range. In this work, correlated electrical and optical detection of single nanoparticles, H1N1 viruses, and λ-DNA molecules was demonstrated. Different types of particles in a mixture were successfully discriminated. Moreover, the flow velocity in the liquid-core channel was extracted with the help of combined analysis of electrical and optical signals. Enhanced electrical sensitivity using a solid-state nanopore with a thin limiting aperture sculpted by SiO2 deposition was also shown.

3-D reconstruction of molecular shape from microcrystal thin sections

1983 ◽  
Vol 41 ◽  
pp. 748-749
Author(s):  
S. Cusack ◽  
J.-C. Jésior
Keyword(s):  
Three Dimensional ◽  
Molecular Shape ◽  
Biological Molecules ◽  
Fourier Space ◽  
Single Particles ◽  
Thin Sections ◽  
Standard Methods ◽  
X Ray ◽  
X Ray Crystallography ◽  
Dimensional Reconstruction

Three-dimensional reconstruction techniques using electron microscopy have been principally developed for application to 2-D arrays (i.e. monolayers) of biological molecules and symmetrical single particles (e.g. helical viruses). However many biological molecules that crystallise form multilayered microcrystals which are unsuitable for study by either the standard methods of 3-D reconstruction or, because of their size, by X-ray crystallography. The grid sectioning technique enables a number of different projections of such microcrystals to be obtained in well defined directions (e.g. parallel to crystal axes) and poses the problem of how best these projections can be used to reconstruct the packing and shape of the molecules forming the microcrystal.Given sufficient projections there may be enough information to do a crystallographic reconstruction in Fourier space. We however have considered the situation where only a limited number of projections are available, as for example in the case of catalase platelets where three orthogonal and two diagonal projections have been obtained (Fig. 1).

Computer Assisted Image Reconstruction of Oligomer Structure

1976 ◽  
Vol 34 ◽  
pp. 472-473
Author(s):  
A.M. Jones ◽  
A. Max Fiskin
Keyword(s):  
Three Dimensional ◽  
Depth Of Field ◽  
Computer Assisted ◽  
Projection Data ◽  
Two Dimensional ◽  
Single Particles ◽  
Dimensional Reconstruction ◽  
Computer Assisted Image ◽  
The Fourier Transform ◽  
Space Approach

If the tilt of a specimen can be varied either by the strategy of observing identical particles orientated randomly or by use of a eucentric goniometer stage, three dimensional reconstruction procedures are available (l). If the specimens, such as small protein aggregates, lack periodicity, direct space methods compete favorably in ease of implementation with reconstruction by the Fourier (transform) space approach (2). Regardless of method, reconstruction is possible because useful specimen thicknesses are always much less than the depth of field in an electron microscope. Thus electron images record the amount of stain in columns of the object normal to the recording plates. For single particles, practical considerations dictate that the specimen be tilted precisely about a single axis. In so doing a reconstructed image is achieved serially from two-dimensional sections which in turn are generated by a series of back-to-front lines of projection data.

New challenges to image processing posed by cryo-Electron microscopy of single particles

1991 ◽  
Vol 49 ◽  
pp. 422-423
Author(s):  
Joachim Frank
Keyword(s):  
Electron Microscopy ◽  
Phase Contrast ◽  
Particle Orientation ◽  
Single Particles ◽  
Contrast Transfer Function ◽  
Virtual Absence ◽  
Cryo Electron Microscopy ◽  
Spatial Frequencies ◽  
New Challenges ◽  
Particle Images

Compared with images of negatively stained single particle specimens, those obtained by cryo-electron microscopy have the following new features: (a) higher “signal” variability due to a higher variability of particle orientation; (b) reduced signal/noise ratio (S/N); (c) virtual absence of low-spatial-frequency information related to elastic scattering, due to the properties of the phase contrast transfer function (PCTF); and (d) reduced resolution due to the efforts of the microscopist to boost the PCTF at low spatial frequencies, in his attempt to obtain recognizable particle images.

Microstructure and reactivity of small metal particles: The role of Ce additives

1992 ◽  
Vol 50 (1) ◽  
pp. 318-319
Author(s):  
L.D. Schmidt ◽  
K. R. Krause ◽  
J. M. Schwartz ◽  
X. Chu
Keyword(s):  
Atmospheric Pressure ◽  
Noble Metals ◽  
Mixed Oxides ◽  
Catalytic Properties ◽  
Chemical Shifts ◽  
Catalytic Converter ◽  
Structural Evolution ◽  
Single Particles ◽  
Small Metal Particles

The evolution of microstructures of 10- to 100-Å diameter particles of Rh and Pt on SiO2 and Al2O3 following treatment in reducing, oxidizing, and reacting conditions have been characterized by TEM. We are able to transfer particles repeatedly between microscope and a reactor furnace so that the structural evolution of single particles can be examined following treatments in gases at atmospheric pressure. We are especially interested in the role of Ce additives on noble metals such as Pt and Rh. These systems are crucial in the automotive catalytic converter, and rare earths can significantly modify catalytic properties in many reactions. In particular, we are concerned with the oxidation state of Ce and its role in formation of mixed oxides with metals or with the support. For this we employ EELS in TEM, a technique uniquely suited to detect chemical shifts with ∼30Å resolution.

Structure of rattlesnake venom lectin determined by single particle high-resolution electron microscopy

1996 ◽  
Vol 54 ◽  
pp. 62-63
Author(s):  
Peter D. Moisiuk ◽  
Daniel R. Beniac ◽  
Ross A. Ridsdale ◽  
Martin Young ◽  
Bhushan Nagar ◽  
...  
Keyword(s):  
High Resolution Electron Microscopy ◽  
Lipid Monolayer ◽  
Outer Diameter ◽  
X Ray Diffraction ◽  
Single Particles ◽  
Crotalus Atrox ◽  
3D Reconstructions ◽  
X Ray ◽  
Rattlesnake Venom ◽  
Covalently Linked

Venom from the rattlesnake Crotalus atrox contains a mixture of enzymes that induce a localized effect leading to hemorrhaging, necrosis and edema. As a member of the crotalid family of snake venoms, Crotalus atrox venom contains a C-type lectin that will agglutinate blood cells in a Ca2+-dependent fashion. The lectin is a hydrophilic protein, consisting of two covalently linked, 135 amino acid residues, identical subunits that are rich in aspartic acid, glutamic acid and lysine. Sequence homology with known carbohydrate recognition domains (CRDs) indicates that rattlesnake venom lectin (RSLV) contains a CRD motif that is not linked to accessory domains. Preliminary X-ray diffraction and sedimentation analysis has indicated that lectin from Crotalus atrox forms decamers composed of two five-fold symmetric pentamers. Single particles of RSVL imaged at – 171°C displayed two distinct orientations on the specimen support (Figure a) following incubation in a crystallization Teflon well, coated with a lipid monolayer consisting of phosphatidylcholine and monosialoganglioside. When lying in an end-on orientation, the lectin exhibited a “pentagonal ring” with an outer diameter of 6.7 nm and an inner hollow core of 1.7 nm. A side orientation was also seen, whereby a thickness of 5.8 nm was measured for the lectin. Image processing of 2280 single particles placed in 100 classes (Figure b) led to 3D reconstructions of RSVL (Figure c). Density limited 3D reconstructions showed the lectin to be made of two five-fold symmetrical rings covalently linked between the five subunits that constitute each ring of this homodimer. These results are consistent with sedimentation and preliminary X-ray diffraction analysis on the shape of RSVL and provide the framework for structural verification by 2D electron crystallography.

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