scholarly journals Three-dimensional reconstruction of an actin bundle.

1988 ◽  
Vol 107 (2) ◽  
pp. 597-611 ◽  
Author(s):  
E S Bullitt ◽  
D J DeRosier ◽  
L M Coluccio ◽  
L G Tilney
Keyword(s):  
Electron Microscopy ◽  
Transmission Electron Microscopy ◽  
Three Dimensional ◽  
Oblate Spheroid ◽  
Potassium Thiocyanate ◽  
Dimensional Structure ◽  
Transmission Electron ◽  
Scanning Transmission ◽  
Dimensional Reconstruction ◽  
Molecular Masses

We present the three-dimensional structure of an actin filament bundle from the sperm of Limulus. The bundle is a motile structure which by changing its twist, converts from a coiled to an extended form. The bundle is composed of actin plus two auxiliary proteins of molecular masses 50 and 60 kD. Fraying the bundle with potassium thiocyanate created three classes of filaments: actin, actin plus the 60-kD protein, and actin plus both the auxiliary proteins. We examined these filaments by transmission electron microscopy and scanning transmission electron microscopy (STEM). Three-dimensional reconstructions from electron micrographs allowed us to visualize the actin subunit and the 60- and 50-kD subunits bound to it. The actin subunit appears to be bilobed with dimensions 70 X 40 X 35 A. The inner lobe of the actin subunit, located at 20 A radius, is a prolate ellipsoid, 50 X 25 A; the outer actin lobe, at 30 A radius, is a 35-A-diam spheroid. Attached to the inner lobe of actin is the 60-kD protein, an oblate spheroid, 55 X 40 A, at 50 A radius. The armlike 50-kD protein, at 55 A radius, links the 60-kD protein on one of actin's twin strands to the outer lobe of the actin subunit on the opposite strand. We speculate that the 60-kD protein may be a bundling protein and that the 50-kD protein may be responsible for the change in twist of the filaments which causes extension of the bundle.

Three-dimensional ADF imaging of individual atoms by through-focal series scanning transmission electron microscopy

2006 ◽  
Vol 106 (11-12) ◽  
pp. 1062-1068 ◽  
Author(s):  
Klaus van Benthem ◽  
Andrew R. Lupini ◽  
Mark P. Oxley ◽  
Scott D. Findlay ◽  
Leslie J. Allen ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Transmission Electron Microscopy ◽  
Scanning Transmission Electron Microscopy ◽  
Three Dimensional ◽  
Scanning Transmission Electron ◽  
Transmission Electron ◽  
Scanning Transmission

Three-Dimensional Imaging of Shear Band Produced by ECAP Process in Al-Ag Alloy

2006 ◽  
Vol 503-504 ◽  
pp. 603-608
Author(s):  
Koji Inoke ◽  
Kenji Kaneko ◽  
Z. Horita
Keyword(s):  
Electron Microscopy ◽  
Transmission Electron Microscopy ◽  
Electron Tomography ◽  
Shear Bands ◽  
Three Dimensional ◽  
Angular Pressing ◽  
Ecap Process ◽  
Transmission Electron ◽  
Scanning Transmission ◽  
The Matrix

A significant change in microstructure occurs during the application of severe plastic deformation (SPD) such as by equal-channel angular pressing (ECAP). In this study, intense plastic strain was imposed on an Al-10.8wt%Ag alloy by the ECAP process. The amount of strain was controlled by the numbers of passes. After 1 pass of ECAP, shear bands became visible within the matrix. With increasing numbers of ECAP passes, the fraction of shear bands was increased. In this study, the change in microstructures was examined by three-dimensional electron tomography (3D-ET) in transmission electron microscopy (TEM) or scanning transmission electron microscopy (STEM). With this 3D-ET method, it was possible to conduct a precise analysis of the sizes, widths and distributions of the shear bands produced by the ECAP process. It is demonstrated that the 3D-ET method is promising to understand mechanisms of microstructural refinement using the ECAP process.

scholarly journals Three-Dimensional Scanning Transmission Electron Microscopy of Biological Specimens

2010 ◽  
Vol 16 (1) ◽  
pp. 54-63 ◽  
Author(s):  
Niels de Jonge ◽  
Rachid Sougrat ◽  
Brian M. Northan ◽  
Stephen J. Pennycook
Keyword(s):  
Electron Microscopy ◽  
Transmission Electron Microscopy ◽  
Mammalian Cells ◽  
Three Dimensional ◽  
Axial Resolution ◽  
Beam Radiation ◽  
Thin Sections ◽  
Scanning Transmission Electron ◽  
Transmission Electron ◽  
Scanning Transmission

AbstractA three-dimensional (3D) reconstruction of the cytoskeleton and a clathrin-coated pit in mammalian cells has been achieved from a focal-series of images recorded in an aberration-corrected scanning transmission electron microscope (STEM). The specimen was a metallic replica of the biological structure comprising Pt nanoparticles 2–3 nm in diameter, with a high stability under electron beam radiation. The 3D dataset was processed by an automated deconvolution procedure. The lateral resolution was 1.1 nm, set by pixel size. Particles differing by only 10 nm in vertical position were identified as separate objects with greater than 20% dip in contrast between them. We refer to this value as the axial resolution of the deconvolution or reconstruction, the ability to recognize two objects, which were unresolved in the original dataset. The resolution of the reconstruction is comparable to that achieved by tilt-series transmission electron microscopy. However, the focal-series method does not require mechanical tilting and is therefore much faster. 3D STEM images were also recorded of the Golgi ribbon in conventional thin sections containing 3T3 cells with a comparable axial resolution in the deconvolved dataset.

Three-Dimensional Structure of Helical and Zigzagged Nanowires Using Electron Tomography

2008 ◽  
Vol 1144 ◽  
Author(s):  
Han Sung Kim ◽  
Yoon Myung ◽  
Chang Hyun Kim ◽  
Seung Yong Bae ◽  
Jae-Pyoung Ahn ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Transmission Electron Microscopy ◽  
High Resolution ◽  
Electron Tomography ◽  
Three Dimensional ◽  
Helical Structure ◽  
Axial Direction ◽  
Dimensional Structure ◽  
Gan Nanowires ◽  
Transmission Electron

ABSTRACTElectron tomography and high-resolution transmission electron microscopy were used to characterize the unique three-dimensional structures of helical or zigzagged GaN, ZnGa2O4 and Zn2SnO4 nanowires. The helical GaN nanowires adopt a helical structure that consists of six equivalent <0-111> growth directions with the axial [0001] direction. The ZnGa2O4 nanosprings have four equivalent <011> growth directions with the [001] axial direction. The zigzagged Zn2SnO4 nanowires consisted of linked rhombohedrons structure having the side edges matched to the <011> direction, and the [111] axial direction.

Sign in / Sign up

Export Citation Format

Share Document