Mythologisms in Novel Interpretations

Recently, it has become essential to develop a helpful method of the complete crystallographic identification of fine fragmented crystals. This was maainly due to the investigation into structural regularity of large plastic strains. The method should be practicable for determining crystallographic orientation (CO) of elastically stressed micro areas of the order of several micron fractions in size and filled with λ>1010 cm-2 density dislocations or stacking faults. The method must provide the misorientation vectors of the adjacent fragments when the angle ω changes from 0 to 180° with the accuracy of 0,3°. The problem is that the actual electron diffraction patterns obtained from fine fragmented crystals are the superpositions of reflections from various fragments, though more than one or two reflections from a fragment are hardly possible. Finally, the method should afford fully automatic computerized processing of the experimental results.The proposed method meets all the above requirements. It implies the construction for a certain base position of the crystal the orientation matrix (0M) A, which gives a single intercorrelation between the coordinates of the unity vector in the reference coordinate system (RCS) and those of the same vector in the crystal reciprocal lattice base : .

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Computer processing of high-resolution images of periodic specimens

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100141834 ◽

1986 ◽

Vol 44 ◽

pp. 2-5

Author(s):

W. Chiu ◽

M.F. Schmid ◽

T.-W. Jeng

Keyword(s):

High Resolution ◽

Fourier Transforms ◽

Complex Structure ◽

Distribution Functions ◽

Multiple Image ◽

Cryo Electron Microscopy ◽

Structure Factors ◽

Unit Cells ◽

High Resolution Images ◽

Phase Probability Distribution

Cryo-electron microscopy has been developed to the point where one can image thin protein crystals to 3.5 Å resolution. In our study of the crotoxin complex crystal, we can confirm this structural resolution from optical diffractograms of the low dose images. To retrieve high resolution phases from images, we have to include as many unit cells as possible in order to detect the weak signals in the Fourier transforms of the image. Hayward and Stroud proposed to superimpose multiple image areas by combining phase probability distribution functions for each reflection. The reliability of their phase determination was evaluated in terms of a crystallographic “figure of merit”. Grant and co-workers used a different procedure to enhance the signals from multiple image areas by vector summation of the complex structure factors in reciprocal space.

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A large rotating structure around AB Doradus A at VLBI scale

Proceedings of the International Astronomical Union ◽

10.1017/s1743921319009785 ◽

2019 ◽

Vol 15 (S354) ◽

pp. 189-194

Author(s):

J. B. Climent ◽

J. C. Guirado ◽

R. Azulay ◽

J. M. Marcaide

Keyword(s):

Magnetic Reconnection ◽

Main Sequence ◽

Complex Structure ◽

Main Sequence Star ◽

Polar Cap ◽

Vlbi Observations ◽

Rotating Structure ◽

Source Structure ◽

Expected Position

AbstractWe report the results of three VLBI observations of the pre-main-sequence star AB Doradus A at 8.4 GHz. With almost three years between consecutive observations, we found a complex structure at the expected position of this star for all epochs. Maps at epochs 2007 and 2010 show a double core-halo morphology while the 2013 map reveals three emission peaks with separations between 5 and 18 stellar radii. Furthermore, all maps show a clear variation of the source structure within the observing time. We consider a number of hypothesis in order to explain such observations, mainly: magnetic reconnection in loops on the polar cap, a more general loop scenario and a close companion to AB Dor A.

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SAC3B is a target of CML19, the centrin 2 of Arabidopsis thaliana

Biochemical Journal ◽

10.1042/bcj20190674 ◽

2020 ◽

Vol 477 (1) ◽

pp. 173-189 ◽

Cited By ~ 1

Author(s):

Marco Pedretti ◽

Carolina Conter ◽

Paola Dominici ◽

Alessandra Astegno

Keyword(s):

Excision Repair ◽

Complex Structure ◽

Binding Motif ◽

C Terminus ◽

Repair Protein ◽

Nucleotide Excision ◽

Ef Hand ◽

Molecular Determinants ◽

Structure In Solution

Arabidopsis centrin 2, also known as calmodulin-like protein 19 (CML19), is a member of the EF-hand superfamily of calcium (Ca2+)-binding proteins. In addition to the notion that CML19 interacts with the nucleotide excision repair protein RAD4, CML19 was suggested to be a component of the transcription export complex 2 (TREX-2) by interacting with SAC3B. However, the molecular determinants of this interaction have remained largely unknown. Herein, we identified a CML19-binding site within the C-terminus of SAC3B and characterized the binding properties of the corresponding 26-residue peptide (SAC3Bp), which exhibits the hydrophobic triad centrin-binding motif in a reversed orientation (I8W4W1). Using a combination of spectroscopic and calorimetric experiments, we shed light on the SAC3Bp–CML19 complex structure in solution. We demonstrated that the peptide interacts not only with Ca2+-saturated CML19, but also with apo-CML19 to form a protein–peptide complex with a 1 : 1 stoichiometry. Both interactions involve hydrophobic and electrostatic contributions and include the burial of Trp residues of SAC3Bp. However, the peptide likely assumes different conformations upon binding to apo-CML19 or Ca2+-CML19. Importantly, the peptide dramatically increases the affinity for Ca2+ of CML19, especially of the C-lobe, suggesting that in vivo the protein would be Ca2+-saturated and bound to SAC3B even at resting Ca2+-levels. Our results, providing direct evidence that Arabidopsis SAC3B is a CML19 target and proposing that CML19 can bind to SAC3B through its C-lobe independent of a Ca2+ stimulus, support a functional role for these proteins in TREX-2 complex and mRNA export.

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Crystal structures of Magnaporthe oryzae trehalose-6-phosphate synthase (MoTps1) suggest a model for catalytic process of Tps1

Biochemical Journal ◽

10.1042/bcj20190289 ◽

2019 ◽

Vol 476 (21) ◽

pp. 3227-3240 ◽

Cited By ~ 1

Author(s):

Shanshan Wang ◽

Yanxiang Zhao ◽

Long Yi ◽

Minghe Shen ◽

Chao Wang ◽

...

Keyword(s):

Crystal Structures ◽

Conformational Changes ◽

Magnaporthe Oryzae ◽

Structural Information ◽

Complex Structure ◽

Critical Role ◽

Catalytic Process ◽

Structural Basis ◽

Salt Bridges ◽

Terminal Domain

Trehalose-6-phosphate (T6P) synthase (Tps1) catalyzes the formation of T6P from UDP-glucose (UDPG) (or GDPG, etc.) and glucose-6-phosphate (G6P), and structural basis of this process has not been well studied. MoTps1 (Magnaporthe oryzae Tps1) plays a critical role in carbon and nitrogen metabolism, but its structural information is unknown. Here we present the crystal structures of MoTps1 apo, binary (with UDPG) and ternary (with UDPG/G6P or UDP/T6P) complexes. MoTps1 consists of two modified Rossmann-fold domains and a catalytic center in-between. Unlike Escherichia coli OtsA (EcOtsA, the Tps1 of E. coli), MoTps1 exists as a mixture of monomer, dimer, and oligomer in solution. Inter-chain salt bridges, which are not fully conserved in EcOtsA, play primary roles in MoTps1 oligomerization. Binding of UDPG by MoTps1 C-terminal domain modifies the substrate pocket of MoTps1. In the MoTps1 ternary complex structure, UDP and T6P, the products of UDPG and G6P, are detected, and substantial conformational rearrangements of N-terminal domain, including structural reshuffling (β3–β4 loop to α0 helix) and movement of a ‘shift region' towards the catalytic centre, are observed. These conformational changes render MoTps1 to a ‘closed' state compared with its ‘open' state in apo or UDPG complex structures. By solving the EcOtsA apo structure, we confirmed that similar ligand binding induced conformational changes also exist in EcOtsA, although no structural reshuffling involved. Based on our research and previous studies, we present a model for the catalytic process of Tps1. Our research provides novel information on MoTps1, Tps1 family, and structure-based antifungal drug design.

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A Structured Method for the Recognition of Complex Historical Tables

History and Computing ◽

10.3366/hac.1997.9.1-3.58 ◽

1997 ◽

Vol 9 (1-3) ◽

pp. 58-77

Author(s):

Vitaly Kliatskine ◽

Eugene Shchepin ◽

Gunnar Thorvaldsen ◽

Konstantin Zingerman ◽

Valery Lazarev

Keyword(s):

Nineteenth Century ◽

Character Recognition ◽

Optical Character Recognition ◽

Complex Structure ◽

Source Material ◽

Historical Sources ◽

Tax Assessment ◽

Optical Character ◽

Algorithmic Model ◽

Machine Readable

In principle, printed source material should be made machine-readable with systems for Optical Character Recognition, rather than being typed once more. Offthe-shelf commercial OCR programs tend, however, to be inadequate for lists with a complex layout. The tax assessment lists that assess most nineteenth century farms in Norway, constitute one example among a series of valuable sources which can only be interpreted successfully with specially designed OCR software. This paper considers the problems involved in the recognition of material with a complex table structure, outlining a new algorithmic model based on ‘linked hierarchies’. Within the scope of this model, a variety of tables and layouts can be described and recognized. The ‘linked hierarchies’ model has been implemented in the ‘CRIPT’ OCR software system, which successfully reads tables with a complex structure from several different historical sources.

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Representation of bolted joints in a structure using finite element modelling and model updating

JOURNAL OF MECHANICAL ENGINEERING AND SCIENCES ◽

10.15282/jmes.14.3.2020.15.0560 ◽

2020 ◽

Vol 14 (3) ◽

pp. 7141-7151 ◽

Cited By ~ 1

Author(s):

R. Omar ◽

M. N. Abdul Rani ◽

M. A. Yunus

Keyword(s):

Finite Element ◽

Dynamic Behaviour ◽

Model Updating ◽

Complex Structure ◽

Bolted Joints ◽

Model Parameters ◽

Fe Model ◽

Bolted Joint ◽

Fe Modelling ◽

Joint Structure

Efficient and accurate finite element (FE) modelling of bolted joints is essential for increasing confidence in the investigation of structural vibrations. However, modelling of bolted joints for the investigation is often found to be very challenging. This paper proposes an appropriate FE representation of bolted joints for the prediction of the dynamic behaviour of a bolted joint structure. Two different FE models of the bolted joint structure with two different FE element connectors, which are CBEAM and CBUSH, representing the bolted joints are developed. Modal updating is used to correlate the two FE models with the experimental model. The dynamic behaviour of the two FE models is compared with experimental modal analysis to evaluate and determine the most appropriate FE model of the bolted joint structure. The comparison reveals that the CBUSH element connectors based FE model has a greater capability in representing the bolted joints with 86 percent accuracy and greater efficiency in updating the model parameters. The proposed modelling technique will be useful in the modelling of a complex structure with a large number of bolted joints.

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Model-Based Shape Optimization of Three-Dimensional Complex Structure for Heat Transfer Enhancement in Single-Phase Flows

Proceedings of the 15th International Heat Transfer Conference ◽

10.1615/ihtc15.hte.008867 ◽

2014 ◽

Author(s):

Yosuke Hasegawa ◽

Naoki Shikazono

Keyword(s):

Heat Transfer ◽

Shape Optimization ◽

Heat Transfer Enhancement ◽

Single Phase ◽

Complex Structure ◽

Three Dimensional ◽

Transfer Enhancement ◽

Model Based

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Morphological Characteristics of the Stroma in Malignat Epithelial Neoplasms with Short Review of Skin Squamous Cell Carcinoma

Macedonian Medical Review ◽

10.2478/mmr-2014-0002 ◽

2014 ◽

Vol 68 (1) ◽

pp. 8-15

Author(s):

Lena Kakasheva-Mazhenkovska ◽

Vesna Janevska ◽

Gordana Petrushevska ◽

Liljana Spasevska ◽

Neli Basheska

Keyword(s):

Immune Cells ◽

Complex Structure ◽

Tumor Development ◽

Morphological Characteristics ◽

Basal Membrane ◽

Short Review ◽

Invasion And Metastasis ◽

Genetic Changes ◽

Cancer Associated Fibroblast ◽

Skin Squamous Cell Carcinoma

Abstract The stroma of the neoplasm is a highly complex structure built by: specialized mesenchymal cells typical for each tissue surroundings, cancer associated fibroblast/myofibroblast, congenital or acquired immune cells, vascular network with endothelial cells and pericytes, mastocytes, macrophages, leukocytes and adipocytes, all together incorporated in the extracellular matrix. Each neoplasm produces its own unique microenvironment where the tumor grows and modifies. Although most of the cells of the host in the stroma have compulsory tumor suppressor ability, the stroma is changing during the malignant process and it even promotes growth, invasion and metastasis. Genetic changes that occur during the development of the cancer, which are guided by the malignant cells lead to changes in the stroma of the host that will overtake it and adjust it to their own needs. In the early stages of the tumor development and invasion, the basal membrane is degraded and the stroma becomes active and contains an increased number of fibroblasts, inflammatory infiltrate and newly composed capillaries which come into direct contact with the tumor cells. These changes lead to cancer invasion.

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