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      Three-dimensional structure of herpes simplex virus from cryo-electron tomography.

      Science (New York, N.Y.)
      Animals, Capsid, chemistry, ultrastructure, Cercopithecus aethiops, Cryoelectron Microscopy, Herpesvirus 1, Human, physiology, Humans, Image Processing, Computer-Assisted, Lipid Bilayers, Nucleocapsid, Tomography, Vero Cells, Viral Envelope Proteins, analysis, Virion

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          Abstract

          Herpes simplex virus, a DNA virus of high complexity, consists of a nucleocapsid surrounded by the tegument-a protein compartment-and the envelope. The latter components, essential for infectivity, are pleiomorphic. Visualized in cryo-electron tomograms of isolated virions, the tegument was seen to form an asymmetric cap: On one side, the capsid closely approached the envelope; on the other side, they were separated by approximately 35 nanometers of tegument. The tegument substructure was particulate, with some short actin-like filaments. The envelope contained 600 to 750 glycoprotein spikes that varied in length, spacing, and in the angles at which they emerge from the membrane. Their distribution was nonrandom, suggesting functional clustering.

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          Paxillin and focal adhesion signalling.

          To facilitate a rapid response to environmental change, cells use scaffolding - or adaptor - proteins to recruit key components of their signal-transduction machinery to specific subcellular locations. Paxillin is a multi-domain adaptor found at the interface between the plasma membrane and the actin cytoskeleton. Here it provides a platform for the integration and processing of adhesion- and growth factor-related signals.
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            Macromolecular architecture in eukaryotic cells visualized by cryoelectron tomography.

            Electron tomography of vitrified cells is a noninvasive three-dimensional imaging technique that opens up new vistas for exploring the supramolecular organization of the cytoplasm. We applied this technique to Dictyostelium cells, focusing on the actin cytoskeleton. In actin networks reconstructed without prior removal of membranes or extraction of soluble proteins, the cross-linking of individual microfilaments, their branching angles, and membrane attachment sites can be analyzed. At a resolution of 5 to 6 nanometers, single macromolecules with distinct shapes, such as the 26S proteasome, can be identified in an unperturbed cellular environment.
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              Noise reduction in electron tomographic reconstructions using nonlinear anisotropic diffusion.

              Electron tomography is a powerful technique capable of giving unique insights into the three-dimensional structural organization of pleomorphic biological objects. However, visualization and interpretation of the resulting volumetric data are hampered by an extremely low signal-to-noise ratio, especially when ice-embedded biological specimens are investigated. Usually, isosurface representation or volume rendering of such data is hindered without any further signal enhancement. We propose a novel technique for noise reduction based on nonlinear anisotropic diffusion. The approach combines efficient noise reduction with excellent signal preservation and is clearly superior to conventional methods (e.g., low-pass and median filtering) and invariant wavelet transform filtering. The gain in the signal-to-noise ratio is verified and demonstrated by means of Fourier shell correlation. Improved visualization performance after processing the 3D images is demonstrated with two examples, tomographic reconstructions of chromatin and of a mitochondrion. Parameter settings and discretization stencils are presented in detail. (c)2001 Elsevier Science.
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