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Transmission electron microscopy negative staining

Tobacco primary cell wall and normal bacterial Acetobacter xylinum cellulose formation produced a 36.8 3A triple-stranded left-hand helical microfibril in freeze-dried Pt-C replicas and in negatively stained preparations for transmission electron microscopy (TEM). A. xylinum growth in the presence of 0.25 mM Tinopal disrupted cellulose microfibril formation and produced a... [Pg.278]

Figure 14.10 Self-assembly of peptide-amphiphiles into nanofibers (a) a peptide amphi-phile molecule with five distinct regions designed for hydroxyapatite mineralization, (b) a schematic of molecular self-assembly, and (c) a negatively stain transmission electron microscopy image of the nanofibers. Reprinted from Hartgerink et al. (2001). Copyright 2001 American Association for the Advancement of Science. Figure 14.10 Self-assembly of peptide-amphiphiles into nanofibers (a) a peptide amphi-phile molecule with five distinct regions designed for hydroxyapatite mineralization, (b) a schematic of molecular self-assembly, and (c) a negatively stain transmission electron microscopy image of the nanofibers. Reprinted from Hartgerink et al. (2001). Copyright 2001 American Association for the Advancement of Science.
Transmission electron microscopy thin-sectioning, negative staining, freeze etching, mica-technique, cryo-TEM Atomic force microscopy... [Pg.81]

Transmission Electron Microscopy (TEM) is perhaps the most used visualization method for studying polymer aggregates. Additionally, negative staining permits very high resolution imaging of surface details. Cryo-TEM offers another advantage since specimens are rapidly frozen and viewed in a natural hydrated state... [Pg.143]

Electron microscopic images of lipoproteins show predominantly spherical shapes. Only nascent HDL appear as stacks of discs by negative-stain transmission electron microscopy. The stacks are artifacts of the method, because in solution nascent HDL... [Pg.501]

Transmission electron microscopy (TEM) Negative staining and metal shadowing Chemical and structural information for liquid foods and emulsions... [Pg.3073]

Figure 9.1 (Top) Structural representations of DMpillar[5]arene and guest G9.1, as well as the proposed mechanism for the formation of vesicular assemblies. (Bottom) Microscopic morphology of the vesicular assemblies formed from the complex between DMpillar[5]arene and G9.1 in Me2CO (1 mM). Negative-stained transmission electron microscopy (TEM) images with scale bars of (a) 1 pm and (b) 0.2 pm. Gold sputtering scaiming electron microscopy (SEM) images with scale bars of (c) 10 pm and (d) 100 nm. Figure 9.1 (Top) Structural representations of DMpillar[5]arene and guest G9.1, as well as the proposed mechanism for the formation of vesicular assemblies. (Bottom) Microscopic morphology of the vesicular assemblies formed from the complex between DMpillar[5]arene and G9.1 in Me2CO (1 mM). Negative-stained transmission electron microscopy (TEM) images with scale bars of (a) 1 pm and (b) 0.2 pm. Gold sputtering scaiming electron microscopy (SEM) images with scale bars of (c) 10 pm and (d) 100 nm.
Figure 20.3. The pili of the lactic acid bacterium Lactococcus lactis affect the architecture of biofilms, (a) Non-piliated L. lactis biofilm and (b) piliated L. lactis biofilm obtained from confocal image series, (c) L lactis pili observed using negative staining and transmission electron microscopy. Images (a) and (b) are from Julien Deschamps and image (c) from Alexis Cannette (http /Awww6.jouy.inra.fr/mima2 eng/). Figure 20.3. The pili of the lactic acid bacterium Lactococcus lactis affect the architecture of biofilms, (a) Non-piliated L. lactis biofilm and (b) piliated L. lactis biofilm obtained from confocal image series, (c) L lactis pili observed using negative staining and transmission electron microscopy. Images (a) and (b) are from Julien Deschamps and image (c) from Alexis Cannette (http /Awww6.jouy.inra.fr/mima2 eng/).
Figure 1 Transmission electron microscopy examination of purified type 2 rAAV particles. HPLC-purified type 2 rAAV particles were negatively stained with 1% aqueous uranyl acetate for 30 sec and processed for transrrussion eleciron microscopy. The image was photographed on a Hitachi H-7000 transmission electron microscope. The insert in the upper left comer is a photomicrograph of a single recombinant adenoviral particle processed under the same conditions. The arrowheads indicate the empty and/or not fully packaged rAAV particles. The 50-nm scale bar applies to both rAAV and adenovirus photomicrographs. Figure 1 Transmission electron microscopy examination of purified type 2 rAAV particles. HPLC-purified type 2 rAAV particles were negatively stained with 1% aqueous uranyl acetate for 30 sec and processed for transrrussion eleciron microscopy. The image was photographed on a Hitachi H-7000 transmission electron microscope. The insert in the upper left comer is a photomicrograph of a single recombinant adenoviral particle processed under the same conditions. The arrowheads indicate the empty and/or not fully packaged rAAV particles. The 50-nm scale bar applies to both rAAV and adenovirus photomicrographs.
Transmission electronic microscopy (TEM). TEM measurements were made on a Jeol JEM -2100 Transmission Electron Microscope operated at an accelerating voltage of 100 kV in the Institut Federatif d Exploration Fonctionnelle des Genomes (Toulouse, France). Samples were negatively stained by a solution of sodium phosphotungstate. [Pg.411]


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