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Microscopy and imaging

Energy Dispersive X-Ray Analysis (EDX, EDAX) Field Emission Microscopy (FEM) [Pg.167]

Scanning Tunneling Microscopy (STM) Photoemission Electron Microscopy (PEEM) Ellipsometry Microscopy for Surface Imaging (EMSI) [Pg.167]

Seeing the surface of a catalyst, preferably in atomic detail, is the ideal of every catalytic chemist. Unfortunately, optical microscopy is of no use for achieving this, simply because the rather long wavelength of visible light (a few hundred nanometers) does not enable features smaller than about one micrometer to be detected. Electron beams offer better opportunities. Development over the past 40 years has resulted in electron microscopes which routinely achieve magnifications on the order of one million times and reveal details with a resolution of about 0.1 nm [1], The technique has become very popular in catalysis, and several reviews offer a good overview of what electron microscopy and related techniques tell us about a catalyst 12-6]. [Pg.167]

Electron microscopy has yielded remarkable pictures, such as the one in Fig. 7.1, which stimulate our imagination of what a reacting molecule sees on approaching a [Pg.167]

Less generally applicable than electron or scanning probe microscopy, but capable of revealing great detail, are field emission and field ion microscopy (FEM and F1M). These techniques are limited to the investigation of sharp metallic tips, however, with the attractive feature that the facets of such tips exhibit a variety of crystallographically different surface orientations, which can be studied simultaneously, for example in gas adsorption and reaction studies. [Pg.168]


Oshida, K., Kogiso, K., Matsubayashi, K., Takeuchi, K., Kobayashi, S., Endo, M., Dressclhaus, M. S., Drcsselhaus, G., Analysis of pore structure of activated carbon fibers using high resolution transmission electron microscopy and image processing, 7. Mater. Res., 1995, 10(10), 2507 2517. [Pg.112]

J. Bloem, M. Veningra, and J. Shepherd, Fully automatic determination of soil bacterium numbers, cell volumes, and frequencies of dividing cells by confocal laser-scanning microscopy and image-analysis, Appl. Environ. Microbiol. 61 926... [Pg.404]

Rosenberg, M. F., Caliaghan, R., Ford, R. C., Higgins, C. F., Structure of the multidrug resistance P-glyco-protein to 2.5 nm resolution determined by electron microscopy and image analysis, J. Biol. Chem. 1997, 272, 10685-10694. [Pg.487]

Haugland, R. P. (1990) Eluorescein substitutes for microscopy and imaging, in Optical Microscopy for Biology (Herman, B. and Jacobson, K., eds.), Wiley-Liss, New York, pp. 143-157. [Pg.104]

We and others have based invasion assays on preformed tumor spheroids generated either in hanging drops (88) or other nonadherent systems (61). These are then transferred to matrix monolayers or embedded in Matrigel and can be analyzed qualitatively or quantitatively, usually by microscopy and image analysis (see also Chapter 16). A96- or 1,536-well spheroid-based... [Pg.241]

Figure 6. Particle size distributions of sorbitol samples obtained using optical microscopy and image analysis. Figure 6. Particle size distributions of sorbitol samples obtained using optical microscopy and image analysis.
Lansford, R., Bearman, G., and Fraser, S. E. 2001. Resolution of multiple green fluorescent protein color variants and dyes using two-photon microscopy and imaging spectroscopy. J. Biomed. Opt. 6(3) 311-18. [Pg.194]

The intimate contact data shown in Figure 7.16 were obtained from three-ply, APC-2, [0°/90o/0o]7- cross-ply laminates that were compression molded in a 76.2 mm (3 in.) square steel mold. The degree of intimate contact of the ply interfaces was measured using scanning acoustic microscopy and image analysis software (Section 7.4). The surface characterization parameters for APC-2 Batch II prepreg in Table 7.2 and the zero-shear-rate viscosity for PEEK resin were input into the intimate contact model for the cross-ply interface. Additional details of the experimental procedures and the viscosity data for PEEK resin are given in Reference 22. [Pg.226]

Pugnaloni, L.A., Matia-Merino, L., Dickinson, E. (2005). Microstructure of acid-induced caseinate gels containing sucrose quantification from confocal microscopy and image analysis. Colloids and Surfaces B Biointerfaces, 42, 211-217. [Pg.228]

Loren, N., Langton, M., Hermansson, A.-M. (1999). Confocal laser scanning microscopy and image analysis of kinetically trapped phase-separated gelatin/maltodextrin gels. Food Hydrocolloids, 13, 185-198. [Pg.299]

Figure 29-1 (A-C) A 1970s view of a bacterial ribosome achieved by electron microscopy and image reconstruction. These interface views show the surfaces that face each other in the 70S ribosome. Figure 29-1 (A-C) A 1970s view of a bacterial ribosome achieved by electron microscopy and image reconstruction. These interface views show the surfaces that face each other in the 70S ribosome.
Figure 30-17 (A) Two-dimensional map of the 260-kDa a subunit of the voltage-gated Na+ channel from the electric eel Electrophorus e/ecfns.438 441 (B) Image of the sodium channel protein obtained by cryo-electron microscopy and image analysis at 1.9 nm resolution. In this side view the protein appears to be bell-shaped with a height of 13.5 nm, a square bottom (cytoplasmic surface) 10 nm on a side, and a hemispherical top with a diameter of 6.5 nm. (C) Bottom view of the protein. (D) Axial section which cuts the bottom, as viewed in (C), approximately along a diagonal. From Sato et al.438 Notice the cavities (dark) and domain structures (light). The black arrow marks a constriction between upper (extracelllar) and lower (cytoplasmic) cavities. White lines indicate approximate position of the lipid bilayer. From Sato et al.i38 Courtesy of Chikara Sato. Figure 30-17 (A) Two-dimensional map of the 260-kDa a subunit of the voltage-gated Na+ channel from the electric eel Electrophorus e/ecfns.438 441 (B) Image of the sodium channel protein obtained by cryo-electron microscopy and image analysis at 1.9 nm resolution. In this side view the protein appears to be bell-shaped with a height of 13.5 nm, a square bottom (cytoplasmic surface) 10 nm on a side, and a hemispherical top with a diameter of 6.5 nm. (C) Bottom view of the protein. (D) Axial section which cuts the bottom, as viewed in (C), approximately along a diagonal. From Sato et al.438 Notice the cavities (dark) and domain structures (light). The black arrow marks a constriction between upper (extracelllar) and lower (cytoplasmic) cavities. White lines indicate approximate position of the lipid bilayer. From Sato et al.i38 Courtesy of Chikara Sato.
McGough, A., Way, M., and DeRosier, D. (1994). Determination of the alpha-actinin-binding site on actin filaments by cryoelectron microscopy and image analysis. [Pg.241]

Raman Microscopy and Imaging Applications to Skin Pharmacology and Wound Healing... [Pg.365]

Vibrational microspectroscopy provides a unique means for molecular level structure characterization of a variety of biological processes associated with skin. For the past several years, this laboratory has utilized Raman and IR spectroscopy, microscopy, and imaging to monitor the biophysics of the skin barrier, mechanisms of drug permeation and metabolism in intact tissue, and, more recently, the complex events that transpire during wound healing in an ex vivo skin model [1-6]. [Pg.365]


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See also in sourсe #XX -- [ Pg.155 ]




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Electron microscopy and structure images

FT-IR Imaging and Microscopy

Fluorescent microscopy and imaging

In-Situ Scanning Probe Microscopies Imaging and Beyond

Microscopy image

Microscopy imaging

NMR imaging and microscopy

Raman Microscopy and Imaging

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