The Prospect of Three-Dimensional Induction Mapping Inside Magnetic Nanostructures by Combining Electron Holography with Electron Tomography

2004 ◽  
Vol 10 (S02) ◽  
pp. 1010-1011 ◽  
Author(s):  
Rafal E Dunin-Borkowski ◽  
Takeshi Kasama
Keyword(s):  
Electron Tomography ◽  
Three Dimensional ◽  
Magnetic Nanostructures ◽  
Electron Holography

Extended abstract of a paper presented at Microscopy and Microanalysis 2004 in Savannah, Georgia, USA, August 1–5, 2004.

Practical electron tomography

1995 ◽  
Vol 53 ◽  
pp. 742-743
Author(s):  
C.L. Woodcock
Keyword(s):  
Electron Tomography ◽  
Tomographic Reconstruction ◽  
Three Dimensional ◽  
3D Shape ◽  
Computational Resources ◽  
Shape Of Particles

Despite the potential of the technique, electron tomography has yet to be widely used by biologists. This is in part related to the rather daunting list of equipment and expertise that are required. Thanks to continuing advances in theory and instrumentation, tomography is now more feasible for the non-specialist. One barrier that has essentially disappeared is the expense of computational resources. In view of this progress, it is time to give more attention to practical issues that need to be considered when embarking on a tomographic project. The following recommendations and comments are derived from experience gained during two long-term collaborative projects.Tomographic reconstruction results in a three dimensional description of an individual EM specimen, most commonly a section, and is therefore applicable to problems in which ultrastructural details within the thickness of the specimen are obscured in single micrographs. Information that can be recovered using tomography includes the 3D shape of particles, and the arrangement and dispostion of overlapping fibrous and membranous structures.

Three-Dimensional reconstruction of isolated centrosomes by automated electron tomography

1994 ◽  
Vol 52 ◽  
pp. 310-311
Author(s):  
M.B. Braunfeld ◽  
M. Moritz ◽  
B.M. Alberts ◽  
J.W. Sedat ◽  
D.A. Agard
Keyword(s):  
Electron Tomography ◽  
Three Dimensional ◽  
Vital Role ◽  
Complex Nature ◽  
Animal Cells ◽  
Microtubule Organizing Center ◽  
Nucleation Sites ◽  
Dimensional Reconstruction ◽  
Organizing Center ◽  
Resolution Model

In animal cells, the centrosome functions as the primary microtubule organizing center (MTOC). As such the centrosome plays a vital role in determining a cell's shape, migration, and perhaps most importantly, its division. Despite the obvious importance of this organelle little is known about centrosomal regulation, duplication, or how it nucleates microtubules. Furthermore, no high resolution model for centrosomal structure exists.We have used automated electron tomography, and reconstruction techniques in an attempt to better understand the complex nature of the centrosome. Additionally we hope to identify nucleation sites for microtubule growth.Centrosomes were isolated from early Drosophila embryos. Briefly, after large organelles and debris from homogenized embryos were pelleted, the resulting supernatant was separated on a sucrose velocity gradient. Fractions were collected and assayed for centrosome-mediated microtubule -nucleating activity by incubating with fluorescently-labeled tubulin subunits. The resulting microtubule asters were then spun onto coverslips and viewed by fluorescence microscopy.

Electron Holographic Nano-Characterization of Gold Catalyst at Interface

2002 ◽  
Vol 727 ◽  
Author(s):  
S. Ichikawa ◽  
T. Akita ◽  
M. Okumura ◽  
M. Haruta ◽  
K. Tanaka
Keyword(s):  
Contact Angle ◽  
Titanium Oxide ◽  
Gold Catalyst ◽  
Three Dimensional ◽  
High Resolution Electron Microscopy ◽  
Electron Holography ◽  
Gold Particles ◽  
Oxide Support ◽  
The Mean ◽  
A Charge

AbstractThe catalytic properties of nanostructured gold catalyst are known to depend on the size of the gold particles and to be activated when the size decreases to a few nanometers. We investigated the size dependence of the three-dimensional nanostructure on the mean inner potential of gold catalysts supported on titanium oxide using electron holography and high-resolution electron microscopy (HREM). The contact angle of the gold particles on the titanium oxide tended to be over 90° for gold particles with a size of over 5 nm, and below 90° for a size of below 2 nm. This decreasing change in the contact angle (morphology) acts to increase the perimeter and hence the area of the interface between the gold and titanium oxide support, which is considered to be an active site for CO oxidation. The mean inner potential of the gold particles also changed as their size decreased. The value of the inner potential of gold, which is approximately 25 V in bulk state, rose to over 40 V when the size of the gold particles was less than 2 nm. This phenomenon indicates the existence of a charge transfer at the interface between gold and titanium oxide. The 3-D structure change and the inner potential change should be attributed to the specific electronic structure at the interface, owing to both the “nano size effect” and the “hetero-interface effect.”

Three-Dimensional Nanoparticle Distribution and Local Curvature of Heterogeneous Catalysts Revealed by Electron Tomography

2007 ◽  
Vol 111 (31) ◽  
pp. 11501-11505 ◽  
Author(s):  
Edmund P. W. Ward ◽  
Timothy J. V. Yates ◽  
José-Jesús Fernández ◽  
David E. W. Vaughan ◽  
Paul A. Midgley
Keyword(s):  
Heterogeneous Catalysts ◽  
Electron Tomography ◽  
Three Dimensional ◽  
Local Curvature ◽  
Nanoparticle Distribution

scholarly journals Capturing Enveloped Viruses on Affinity Grids for Downstream Cryo-Electron Microscopy Applications

2013 ◽  
Vol 20 (1) ◽  
pp. 164-174 ◽  
Author(s):  
Gabriella Kiss ◽  
Xuemin Chen ◽  
Melinda A. Brindley ◽  
Patricia Campbell ◽  
Claudio L. Afonso ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Measles Virus ◽  
Influenza A ◽  
Electron Tomography ◽  
Three Dimensional ◽  
Nitrilotriacetic Acid ◽  
Dimensional Structure ◽  
Enveloped Viruses ◽  
Cryo Electron Microscopy ◽  
Human Immunodeficiency Virus Virus

AbstractElectron microscopy (EM), cryo-electron microscopy (cryo-EM), and cryo-electron tomography (cryo-ET) are essential techniques used for characterizing basic virus morphology and determining the three-dimensional structure of viruses. Enveloped viruses, which contain an outer lipoprotein coat, constitute the largest group of pathogenic viruses to humans. The purification of enveloped viruses from cell culture presents certain challenges. Specifically, the inclusion of host-membrane-derived vesicles, the complete destruction of the viruses, and the disruption of the internal architecture of individual virus particles. Here, we present a strategy for capturing enveloped viruses on affinity grids (AG) for use in both conventional EM and cryo-EM/ET applications. We examined the utility of AG for the selective capture of human immunodeficiency virus virus-like particles, influenza A, and measles virus. We applied nickel-nitrilotriacetic acid lipid layers in combination with molecular adaptors to selectively adhere the viruses to the AG surface. This further development of the AG method may prove essential for the gentle and selective purification of enveloped viruses directly onto EM grids for ultrastructural analyses.

scholarly journals High-resolution three-dimensional probes of biomaterials and their interfaces

2012 ◽  
Vol 370 (1963) ◽  
pp. 1337-1351 ◽  
Author(s):  
Kathryn Grandfield ◽  
Anders Palmquist ◽  
Håkan Engqvist
Keyword(s):  
High Resolution ◽  
Electron Tomography ◽  
Three Dimensional ◽  
Controlled Drug Release ◽  
Biological Tissues ◽  
Dimensional Structure ◽  
Bone Interface ◽  
Biomaterial Interfaces ◽  
Titania Coating

Interfacial relationships between biomaterials and tissues strongly influence the success of implant materials and their long-term functionality. Owing to the inhomogeneity of biological tissues at an interface, in particular bone tissue, two-dimensional images often lack detail on the interfacial morphological complexity. Furthermore, the increasing use of nanotechnology in the design and production of biomaterials demands characterization techniques on a similar length scale. Electron tomography (ET) can meet these challenges by enabling high-resolution three-dimensional imaging of biomaterial interfaces. In this article, we review the fundamentals of ET and highlight its recent applications in probing the three-dimensional structure of bioceramics and their interfaces, with particular focus on the hydroxyapatite–bone interface, titanium dioxide–bone interface and a mesoporous titania coating for controlled drug release.

An Ultra-High-Tilt Two-Contact Electrical Biasing Specimen Holder for Electron Holography and Electron Tomography of Semiconductor Devices

2004 ◽  
Vol 10 (S02) ◽  
pp. 1012-1013 ◽  
Author(s):  
Rafal E Dunin-Borkowski ◽  
Alison C Twitchett ◽  
Jonathan S Barnard ◽  
Ronald F Broom ◽  
Paul A Midgley ◽  
...  
Keyword(s):  
Electron Tomography ◽  
Semiconductor Devices ◽  
Electron Holography ◽  
Specimen Holder

Extended abstract of a paper presented at Microscopy and Microanalysis 2004 in Savannah, Georgia, USA, August 1–5, 2004.

scholarly journals Distinct roles for antiparallel microtubule pairing and overlap during early spindle assembly

2013 ◽  
Vol 24 (20) ◽  
pp. 3238-3250 ◽  
Author(s):  
Elena Nazarova ◽  
Eileen O'Toole ◽  
Susi Kaitna ◽  
Paul Francois ◽  
Mark Winey ◽  
...  
Keyword(s):  
Electron Tomography ◽  
Dynamical Behavior ◽  
Three Dimensional ◽  
Spindle Assembly ◽  
Intermediate Step ◽  
High Angle ◽  
Normal Number ◽  
Spindle Poles ◽  
Evolutionarily Conserved ◽  
Microtubule Formation

During spindle assembly, microtubules may attach to kinetochores or pair to form antiparallel pairs or interpolar microtubules, which span the two spindle poles and contribute to mitotic pole separation and chromosome segregation. Events in the specification of the interpolar microtubules are poorly understood. Using three-dimensional electron tomography and analysis of spindle dynamical behavior in living cells, we investigated the process of spindle assembly. Unexpectedly, we found that the phosphorylation state of an evolutionarily conserved Cdk1 site (S360) in γ-tubulin is correlated with the number and organization of interpolar microtubules. Mimicking S360 phosphorylation (S360D) results in bipolar spindles with a normal number of microtubules but lacking interpolar microtubules. Inhibiting S360 phosphorylation (S360A) results in spindles with interpolar microtubules and high-angle, antiparallel microtubule pairs. The latter are also detected in wild-type spindles <1 μm in length, suggesting that high-angle microtubule pairing represents an intermediate step in interpolar microtubule formation. Correlation of spindle architecture with dynamical behavior suggests that microtubule pairing is sufficient to separate the spindle poles, whereas interpolar microtubules maintain the velocity of pole displacement during early spindle assembly. Our findings suggest that the number of interpolar microtubules formed during spindle assembly is controlled in part through activities at the spindle poles.

Three-Dimensional Imaging of In Situ Specimens with Low-Dose Electron Tomography to Analyze Protein Conformation

2004 ◽  
Vol 2 (5) ◽  
pp. 561-567 ◽  
Author(s):  
Martina Banyay ◽  
Fredrik Gilstring ◽  
Elenor Hauzenberger ◽  
Lars-Göran Öfverstedt ◽  
Anders B. Eriksson ◽  
...  
Keyword(s):  
Protein Conformation ◽  
Low Dose ◽  
Electron Tomography ◽  
Three Dimensional ◽  
Three Dimensional Imaging

scholarly journals A guided approach for subtomogram averaging of challenging macromolecular assemblies

2020 ◽  
Author(s):  
Danielle Grotjahn ◽  
Saikat Chowdhury ◽  
Gabriel C. Lander
Keyword(s):  
Electron Tomography ◽  
A Priori ◽  
Three Dimensional ◽  
Structural Heterogeneity ◽  
Dimensional Structure ◽  
Diverse Range ◽  
Macromolecular Assemblies ◽  
Cryo Electron Tomography ◽  
Subtomogram Averaging

AbstractCryo-electron tomography is a powerful biophysical technique enabling three-dimensional visualization of complex biological systems. Macromolecular targets of interest identified within cryo-tomograms can be computationally extracted, aligned, and averaged to produce a better-resolved structure through a process called subtomogram averaging (STA). However, accurate alignment of macromolecular machines that exhibit extreme structural heterogeneity and conformational flexibility remains a significant challenge with conventional STA approaches. To expand the applicability of STA to a broader range of pleomorphic complexes, we developed a user-guided, focused refinement approach that can be incorporated into the standard STA workflow to facilitate the robust alignment of particularly challenging samples. We demonstrate that it is possible to align visually recognizable portions of multi-subunit complexes by providing a priori information regarding their relative orientations within cryo-tomograms, and describe how this strategy was applied to successfully elucidate the first three-dimensional structure of the dynein-dynactin motor protein complex bound to microtubules. Our approach expands the application of STA for solving a more diverse range of heterogeneous biological structures, and establishes a conceptual framework for the development of automated strategies to deconvolve the complexity of crowded cellular environments and improve in situ structure determination technologies.

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