Triangulation of Three-Dimensional Aggregate Particles

2009 ◽  
Author(s):  
D. Rypl
Keyword(s):  
Three Dimensional ◽  
Aggregate Particles

Three-Dimensional Image Analysis of Aggregate Particles from Orthogonal Projections

1996 ◽  
Vol 1526 (1) ◽  
pp. 98-103 ◽  
Author(s):  
C.-Y. Kuo ◽  
J.D. Frost ◽  
J.S. Lai ◽  
L.B. Wang
Keyword(s):  
Image Analysis ◽  
Three Dimensional ◽  
Two Dimensional ◽  
Uniform Size ◽  
Standard Size ◽  
Orthogonal Projections ◽  
Projected Image ◽  
Dimensional Image ◽  
Area And Perimeter ◽  
Aggregate Particles

Digital image analysis provides the capability for rapid measurement of particle characteristics. When an image is captured and digitized, numerous measurements can be made in near real time for each particle. Usually, image analysis techniques treat particles as two-dimensional objects since only the two-dimensional projection of the particles is captured. In this study, three-dimensional analysis of aggregate particles that was performed by attaching aggregates in sample trays with two perpendicular faces is described. After the initial projected image of the aggregates is captured and measured, the sample trays are rotated 90 degrees so that the aggregates are now perpendicular to their original orientation and the dimensions of the aggregates in the new projected image are captured and measured. The long, intermediate, and short particle dimensions ( dL, dI, and dS, respectively) provide direct measures of the flatness and elongation of the particles. Some other shape indexes can also be derived from the measurements of area and perimeter length. The proposed image analysis method was verified by comparing the results obtained with manual measurements of particle dimensions for uniform size [passing 12.7 mm (1/2 in.) sieve and retained on 9.5 mm (3/8 in.) sieve] aggregates. Three-dimensional image analysis was also performed on five aggregates of standard size No. 89 from different sources, and the results are summarized herein. The proposed method is expected to improve field quality control of aggregates used in hot mix asphalt.

Wavelet-Based Three-Dimensional Descriptors of Aggregate Particles

2002 ◽  
Vol 1787 (1) ◽  
pp. 109-116 ◽  
Author(s):  
Hyoungkwan Kim ◽  
Carl T. Haas ◽  
Alan F. Rauch ◽  
Craig Browne
Keyword(s):  
Three Dimensional ◽  
Aggregate Particles

The orbit of Pluto over a long interval of time

1966 ◽  
Vol 25 ◽  
pp. 227-229 ◽  
Author(s):  
D. Brouwer
Keyword(s):  
Periodic Orbit ◽  
Numerical Integration ◽  
Restricted Problem ◽  
Three Dimensional ◽  
The Third ◽  
Circular Restricted Problem ◽  
Resonance Relation

The paper presents a summary of the results obtained by C. J. Cohen and E. C. Hubbard, who established by numerical integration that a resonance relation exists between the orbits of Neptune and Pluto. The problem may be explored further by approximating the motion of Pluto by that of a particle with negligible mass in the three-dimensional (circular) restricted problem. The mass of Pluto and the eccentricity of Neptune's orbit are ignored in this approximation. Significant features of the problem appear to be the presence of two critical arguments and the possibility that the orbit may be related to a periodic orbit of the third kind.

Conformation of Ribosomes from Escherichia Coli

1974 ◽  
Vol 32 ◽  
pp. 210-211
Author(s):  
M. Boublik ◽  
W. Hellmann ◽  
F. Jenkins
Keyword(s):  
Binding Sites ◽  
Ribosomal Proteins ◽  
Fluorescent Dyes ◽  
Protein Biosynthesis ◽  
Three Dimensional ◽  
Spatial Arrangement ◽  
Dimensional Structure ◽  
Complete Understanding ◽  
And Function

The present knowledge of the three-dimensional structure of ribosomes is far too limited to enable a complete understanding of the various roles which ribosomes play in protein biosynthesis. The spatial arrangement of proteins and ribonuclec acids in ribosomes can be analysed in many ways. Determination of binding sites for individual proteins on ribonuclec acid and locations of the mutual positions of proteins on the ribosome using labeling with fluorescent dyes, cross-linking reagents, neutron-diffraction or antibodies against ribosomal proteins seem to be most successful approaches. Structure and function of ribosomes can be correlated be depleting the complete ribosomes of some proteins to the functionally inactive core and by subsequent partial reconstitution in order to regain active ribosomal particles.

Ultrastructural Investigations of the Contractile Filaments of Amoebae

1974 ◽  
Vol 32 ◽  
pp. 188-189
Author(s):  
P.L. Moore
Keyword(s):  
Cytoplasmic Streaming ◽  
Three Dimensional ◽  
Freeze Fracture ◽  
Amoeboid Movement ◽  
Different Types ◽  
Chemical Conditions ◽  
Complete Interpretation

Previous freeze fracture results on the intact giant, amoeba Chaos carolinensis indicated the presence of a fibrillar arrangement of filaments within the cytoplasm. A complete interpretation of the three dimensional ultrastructure of these structures, and their possible role in amoeboid movement was not possible, since comparable results could not be obtained with conventional fixation of intact amoebae. Progress in interpreting the freeze fracture images of amoebae required a more thorough understanding of the different types of filaments present in amoebae, and of the ways in which they could be organized while remaining functional.The recent development of a calcium sensitive, demembranated, amoeboid model of Chaos carolinensis has made it possible to achieve a better understanding of such functional arrangements of amoeboid filaments. In these models the motility of demembranated cytoplasm can be controlled in vitro, and the chemical conditions necessary for contractility, and cytoplasmic streaming can be investigated. It is clear from these studies that “fibrils” exist in amoeboid models, and that they are capable of contracting along their length under conditions similar to those which cause contraction in vertebrate muscles.

Structural organization of escherichia coli ribosomes as determined by immuno electron microscopy

1978 ◽  
Vol 36 (2) ◽  
pp. 166-167 ◽  
Author(s):  
G. Stöffler ◽  
R.W. Bald ◽  
J. Dieckhoff ◽  
H. Eckhard ◽  
R. Lührmann ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Escherichia Coli ◽  
Ribosomal Proteins ◽  
Structural Organization ◽  
Three Dimensional ◽  
Ribosomal Subunit ◽  
Spatial Arrangement ◽  
Small Subunit ◽  
Antibody Binding ◽  
Immuno Electron Microscopy

A central step towards an understanding of the structure and function of the Escherichia coli ribosome, a large multicomponent assembly, is the elucidation of the spatial arrangement of its 54 proteins and its three rRNA molecules. The structural organization of ribosomal components has been investigated by a number of experimental approaches. Specific antibodies directed against each of the 54 ribosomal proteins of Escherichia coli have been performed to examine antibody-subunit complexes by electron microscopy. The position of the bound antibody, specific for a particular protein, can be determined; it indicates the location of the corresponding protein on the ribosomal surface.The three-dimensional distribution of each of the 21 small subunit proteins on the ribosomal surface has been determined by immuno electron microscopy: the 21 proteins have been found exposed with altogether 43 antibody binding sites. Each one of 12 proteins showed antibody binding at remote positions on the subunit surface, indicating highly extended conformations of the proteins concerned within the 30S ribosomal subunit; the remaining proteins are, however, not necessarily globular in shape (Fig. 1).

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