Three-dimensional PET emission scan registration and transmission scan synthesis

1997 ◽  
Vol 16 (5) ◽  
pp. 542-561 ◽  
Author(s):  
Chung-Lin Huang ◽  
Wen-Tsang Chang ◽  
Liang-Chih Wu ◽  
Jiunn-Kuen Wang
Keyword(s):  
Three Dimensional ◽  
Transmission Scan ◽  
Scan Registration

A novel scan registration method based on the feature-less global descriptor – spherical entropy image

2017 ◽  
Vol 44 (4) ◽  
pp. 552-563 ◽  
Author(s):  
Bo Sun ◽  
Yadan Zeng ◽  
Houde Dai ◽  
Junhao Xiao ◽  
Jianwei Zhang
Keyword(s):  
Mobile Robotics ◽  
High Reliability ◽  
Three Dimensional ◽  
Point Clouds ◽  
Registration Method ◽  
Content Type ◽  
Spherical Fourier Transform ◽  
3D Point Clouds ◽  
3D Data Processing ◽  
Scan Registration

Purpose This paper aims to present the spherical entropy image (SEI), a novel global descriptor for the scan registration of three-dimensional (3D) point clouds. This paper also introduces a global feature-less scan registration strategy based on SEI. It is advantageous for 3D data processing in the scenarios such as mobile robotics and reverse engineering. Design/methodology/approach The descriptor works through representing the scan by a spherical function named SEI, whose properties allow to decompose the six-dimensional transformation into 3D rotation and 3D translation. The 3D rotation is estimated by the generalized convolution theorem based on the spherical Fourier transform of SEI. Then, the translation recovery is determined by phase only matched filtering. Findings No explicit features and planar segments should be contained in the input data of the method. The experimental results illustrate the parameter independence, high reliability and efficiency of the novel algorithm in registration of feature-less scans. Originality/value A novel global descriptor (SEI) for the scan registration of 3D point clouds is presented. It inherits both descriptive power of signature-based methods and robustness of histogram-based methods. A high reliability and efficiency registration method of scans based on SEI is also demonstrated.

scholarly journals Three-dimensional Scan Registration using Curvelet Features in Planetary Environments

2015 ◽  
Vol 33 (2) ◽  
pp. 243-259 ◽  
Author(s):  
Siddhant Ahuja ◽  
Peter Iles ◽  
Steven L. Waslander
Keyword(s):  
Three Dimensional ◽  
Planetary Environments ◽  
Scan Registration

Robust and fast 3-D scan registration using normal distributions transform with supervoxel segmentation

Robotica ◽  
2014 ◽  
Vol 34 (7) ◽  
pp. 1630-1658 ◽  
Author(s):  
Ji W. Kim ◽  
Beom H. Lee
Keyword(s):  
Normal Distribution ◽  
Euclidean Distance ◽  
Three Dimensional ◽  
Surface Structures ◽  
Regular Grid ◽  
Local Surface ◽  
Normal Distributions ◽  
Registration Algorithm ◽  
Scan Registration ◽  
Real World Datasets

SUMMARYThis paper presents what is termed as the supervoxel normal distributions transform (SV-NDT), a novel three-dimensional (3-D) registration algorithm which improves the performance of the three-dimensional normal distributions transform (3-D NDT) significantly. The 3-D NDT partitions a model scan using a 3-D regular grid. Generating normal distributions using the 3-D regular grid causes considerable information loss because the 3-D regular grid does not use any information pertaining to the local surface structures of the model scan. The best type of surface (the constituent unit of each scan) for modeling with one normal distribution is known to be the plane. The SV-NDT reduces the loss of information using a supervoxel-generating algorithm at the partitioning stage. In addition, it uses the information of the local surface structures from the data scan by replacing the Euclidean distance with a function that uses local geometries as well as the Euclidean distance when each point in the data scan is matched to the corresponding normal distribution. Experiments demonstrate that the use of the supervoxel-generating algorithm increases the modeling accuracy of the normal distributions and that the proposed 3-D registration algorithm outperforms the 3-D NDT and other widely used 3-D registration algorithms in terms of robustness and speed on both synthetic and real-world datasets. Additionally, the effect of changing the function to create correspondences is also verified.

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).

Ribosome Structural Organization

1974 ◽  
Vol 32 ◽  
pp. 332-333
Author(s):  
James A. Lake
Keyword(s):  
Ribosomal Proteins ◽  
Structural Organization ◽  
Three Dimensional ◽  
Small Subunit ◽  
Structural Studies ◽  
X Ray Diffraction ◽  
Specific Antibodies ◽  
X Ray ◽  
E Coli ◽  
Complete Sequences

The understanding of ribosome structure has advanced considerably in the last several years. Biochemists have characterized the constituent proteins and rRNA's of ribosomes. Complete sequences have been determined for some ribosomal proteins and specific antibodies have been prepared against all E. coli small subunit proteins. In addition, a number of naturally occuring systems of three dimensional ribosome crystals which are suitable for structural studies have been observed in eukaryotes. Although the crystals are, in general, too small for X-ray diffraction, their size is ideal for electron microscopy.

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