400 Kv Electron Cryo-Microscopic Imaging Of Large Icosahedral Viruses Towards Atomic Resolution

1999 ◽  
Vol 5 (S2) ◽  
pp. 186-187
Author(s):  
Joanita Jakarta ◽  
Wah Chiu
Keyword(s):  
High Resolution ◽  
Three Dimensional ◽  
Clinical Manifestations ◽  
Image Data ◽  
Chromatic Aberration ◽  
Dimensional Structure ◽  
Depth Of Field ◽  
Periodic Arrays ◽  
Icosahedral Viruses ◽  
Simplex Virus

Three-dimensional structure studies provide important information about the organization of macromolecules, often revealing biological mechanisms and protein structure-function relationships. 400 KV electron cryo-microscopy is an emerging technology that is proving to be a powerful tool for studying the structures of large macromolecular assemblies that are often not tractable using other techniques. Its large depth of field makes it well-suited for imaging large objects to high resolution. In addition, a high accelerating voltage minimizes chromatic aberration yielding images of higher contrast. Recently a 400 KV electron cryo-microscope has been used to image periodic arrays of tubulin to 3.5 Å and single particles at somewhat lower resolutions (13 Å) providing practical demonstrations of its usefulness in modern structural biology. In this paper we present high resolution image data of two large icosahedral viruses: herpes simplex virus IB nucleocapsid (HSV IB) and rice dwarf virus (RDV). Human herpes virus (HSV) is associated with a spectrum of diseases ranging from cold sores to more severe clinical manifestations such as mental retardation.

scholarly journals Lattice filter for processing image data of three-dimensional protein nanocrystals

2016 ◽  
Vol 72 (1) ◽  
pp. 34-39 ◽  
Author(s):  
E. van Genderen ◽  
Y.-W. Li ◽  
I. Nederlof ◽  
J. P. Abrahams
Keyword(s):  
Maximum Likelihood ◽  
High Resolution ◽  
Structure Determination ◽  
Fourier Transformation ◽  
Three Dimensional ◽  
Image Data ◽  
Crystalline Lattice ◽  
Dimensional Structure ◽  
Lattice Filter ◽  
Wiener Type

When 300 kV cryo-EM images at Scherzer focus are acquired from ∼100 nm thick three-dimensional protein nanocrystals using a Falcon 2 direct electron detector, Fourier transformation can reveal the crystalline lattice to surprisingly high resolutions, even though the images themselves seem to be devoid of any contrast. Here, it is reported how this lattice information can be enhanced by means of a wave finder in combination with Wiener-type maximum-likelihood filtering. This procedure paves the way towards full three-dimensional structure determination at high resolution for protein crystals.

Electron crystallographic determination of the 3-D structure of staurolite at atomic resolution

1991 ◽  
Vol 49 ◽  
pp. 540-541
Author(s):  
Kenneth H. Downing ◽  
Hu Meisheng ◽  
Hans-Rudolf Went ◽  
Michael A. O'Keefe
Keyword(s):  
High Resolution ◽  
Three Dimensional ◽  
High Resolution Electron Microscopy ◽  
Atomic Resolution ◽  
Dimensional Structure ◽  
Structure Information ◽  
Resolution Electron ◽  
Scattering Effects ◽  
High Resolution Images ◽  
Effects Of Radiation

With current advances in electron microscope design, high resolution electron microscopy has become routine, and point resolutions of better than 2Å have been obtained in images of many inorganic crystals. Although this resolution is sufficient to resolve interatomic spacings, interpretation generally requires comparison of experimental images with calculations. Since the images are two-dimensional representations of projections of the full three-dimensional structure, information is invariably lost in the overlapping images of atoms at various heights. The technique of electron crystallography, in which information from several views of a crystal is combined, has been developed to obtain three-dimensional information on proteins. The resolution in images of proteins is severely limited by effects of radiation damage. In principle, atomic-resolution, 3D reconstructions should be obtainable from specimens that are resistant to damage. The most serious problem would appear to be in obtaining high-resolution images from areas that are thin enough that dynamical scattering effects can be ignored.

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.

The Study on the Clinical Phenotype and Function of HPRT1 Gene

2021 ◽  
Author(s):  
Miao Guo ◽  
Yucai Chen ◽  
Longlong Lin ◽  
Yilin Wang ◽  
Anqi Wang ◽  
...  
Keyword(s):  
Three Dimensional ◽  
Clinical Manifestations ◽  
Protein Translation ◽  
Dimensional Structure ◽  
Normal Individuals ◽  
Second Generation Sequencing ◽  
Self Harm ◽  
And Function ◽  
Neurogenetic Disease ◽  
Generation Sequencing

Abstract Background: Lesch-Nyhan disease (LND) is a rare x-linked purine metabolic neurogenetic disease caused by enzyme hypoxanthine-guanine phosphoriribosyltransferase(HGprt) deficiency, also known as self-destructive appearance syndrome. A series of manifestations are caused by abnormal purine metabolism. The typical clinical manifestations are hyperuricemia, growth retardation, mental retardation, short stature, dance-like athetosis, aggressive behavior, and compulsive self-harm.. Results: we identified a point mutation c.151C > T (p. Arg51*) in a pedigree. We analyzed the clinical characteristics of children in a family, and obtained the blood of their parents and siblings for second-generation sequencing. At the same time, we also analyzed and compared the expression of HPRT1 gene and predicted the three-dimensional structure of the protein. And we analyzed the clinical manifestations caused by the defect of the HPRT1 genethe mutation led to the termination of transcription at the 51st arginine, resulting in the production of truncated protein, and the relative expression of HPRT1 gene in patients was significantly lower than other family members and 10 normal individuals. Conclusion: this mutation leads to the early termination of protein translation and the formation of a truncated HPRT protein, which affects the function of the protein and generates corresponding clinical manifestations.

scholarly journals Extended Dual-Focus Microscopy for Ratiometric-Based 3D Movement Tracking

2020 ◽  
Vol 10 (18) ◽  
pp. 6243
Author(s):  
Seohyun Lee ◽  
Hyuno Kim ◽  
Hideo Higuchi
Keyword(s):  
Drug Delivery ◽  
High Resolution ◽  
Optical Axis ◽  
Three Dimensional ◽  
Virus Transmission ◽  
Living Cells ◽  
Depth Of Field ◽  
Objective Lens ◽  
Accurate Localization ◽  
Movement Tracking

Imaging the three-dimensional movement of small organelles in living cells can provide key information for the dynamics of drug delivery and virus transmission in biomedical disciplines. To stably monitor such intracellular motion using microscope, long depth of field along optical axis and accurate three-dimensional tracking are simultaneously required. In the present work, we suggest an extended dual-focus optics microscopy system by combining a bifocal plane imaging scheme and objective lens oscillation, which enables accurate localization for a long axial range. The proposed system exploits high-resolution functionality by concatenating partial calibration result acquired each axial imaging level, maintaining the practical advantages of ratiometric method.

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