Meticulous Depiction and Genetic Mechanism of Unconformity Belt Structure

Current research on unconformity belt mainly concentrates on the analysis and description of unconformity surface and contact relationship with overlying and underlying strata. Too much emphasis on the division of the “three-layer structure” of unconformity yields obvious disadvantages, i.e., that studies are not only insufficient in the authenticity of architecture but also in the characterization of the combination of the two- and three-dimensional perspectives. Thus, the analysis of genetic mechanism and meticulous depiction is ignored. Accordingly, by making full use of the outcrops and combining previous research findings, this study aims to provide a detailed description and analysis for the unconformity belt structure, and points out the non-uniqueness of the three-layer structure of the unconformity belt. Based on the theory of depositional process and according to the method and principle of the “point-line-surface”, a comprehensive characterization method combined with a kind of “two-dimensional structure” and “three-dimensional structure” is proposed. A two-dimensional structure is a kind of surface structure, while the three-dimensional structure is a kind of body structure, Moreover, this study discusses the recognition significance of the visual unconformity line and visual unconformity surface with respect to the unconformity belt structure. According to the spatial allocation and geological significance of the unconformity belt, two types of models are established in order to depict the structure of unconformity belt better. Combined with the structural elements of the unconformity belt and complied from the viewpoint of the sedimentary environment, the formation mechanism of two-and three-dimensional structures is summarized.

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Three-Dimensional Structure of Cloned T3 Connector Protein at 1.6nm Resolution

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100180161 ◽

1990 ◽

Vol 48 (1) ◽

pp. 282-283

Author(s):

José L. Carrascosa ◽

José M. Valpuesta ◽

Hisao Fujisawa

Keyword(s):

Dna Sequences ◽

Expression Vector ◽

Three Dimensional ◽

Deae Cellulose ◽

Dna Packaging ◽

Dimensional Structure ◽

Two Dimensional ◽

Freezing And Thawing ◽

Three Dimensional Structure ◽

Dimensional Reconstruction

The head to tail connector of bacteriophages plays a fundamental role in the assembly of viral heads and DNA packaging. In spite of the absence of sequence homology, the structure of connectors from different viruses (T4, Ø29, T3, P22, etc) share common morphological features, that are most clearly revealed in their three-dimensional structure. We have studied the three-dimensional reconstruction of the connector protein from phage T3 (gp 8) from tilted view of two dimensional crystals obtained from this protein after cloning and purification.DNA sequences including gene 8 from phage T3 were cloned, into Bam Hl-Eco Rl sites down stream of lambda promotor PL, in the expression vector pNT45 under the control of cI857. E R204 (pNT89) cells were incubated at 42°C for 2h, harvested and resuspended in 20 mM Tris HC1 (pH 7.4), 7mM 2 mercaptoethanol, ImM EDTA. The cells were lysed by freezing and thawing in the presence of lysozyme (lmg/ml) and ligthly sonicated. The low speed supernatant was precipitated by ammonium sulfate (60% saturated) and dissolved in the original buffer to be subjected to gel nitration through Sepharose 6B, followed by phosphocellulose colum (Pll) and DEAE cellulose colum (DE52). Purified gp8 appeared at 0.3M NaCl and formed crystals when its concentration increased above 1.5 mg/ml.

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Three-dimensional structure of bovine heart NADH: ubiquinone oxidoreductase (complex I) by electron microscopy of a single negatively stained two-dimensional crystal

Microscopy ◽

10.1093/jmicro/dft082 ◽

2014 ◽

Vol 63 (2) ◽

pp. 167-174 ◽

Cited By ~ 9

Author(s):

Satoru Shimada ◽

Kyoko Shinzawa-Itoh ◽

Satoko Amano ◽

Yui Akira ◽

Atsuo Miyazawa ◽

...

Keyword(s):

Electron Microscopy ◽

Complex I ◽

Three Dimensional ◽

Dimensional Structure ◽

Two Dimensional ◽

Three Dimensional Structure ◽

Ubiquinone Oxidoreductase ◽

Bovine Heart ◽

Nadh Ubiquinone Oxidoreductase ◽

Dimensional Crystal

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[7] Three-dimensional structure of membrane proteins determined by two-dimensional crystallization, electron cryomicroscopy, and image analysis

Methods in Enzymology - Ion Channels Part C ◽

10.1016/s0076-6879(99)94010-7 ◽

1999 ◽

pp. 135-180 ◽

Cited By ~ 32

Author(s):

Mark Yeager ◽

Vinzenz M. Unger ◽

Alok K. Mitra

Keyword(s):

Image Analysis ◽

Membrane Proteins ◽

Three Dimensional ◽

Dimensional Structure ◽

Two Dimensional ◽

Electron Cryomicroscopy ◽

Three Dimensional Structure

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Three-dimensional structure determination by electron microscopy of two-dimensional crystals

Progress in Biophysics and Molecular Biology ◽

10.1016/0079-6107(83)90017-2 ◽

1982 ◽

Vol 39 ◽

pp. 183-231 ◽

Cited By ~ 403

Author(s):

L.A. Amos ◽

Richard Henderson ◽

P.N.T. Unwin

Keyword(s):

Electron Microscopy ◽

Structure Determination ◽

Three Dimensional ◽

Dimensional Structure ◽

Two Dimensional ◽

Three Dimensional Structure

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Assembled structures of tetrakis(biimidazole)dirhodium complexes hydrogen-bonded with common inorganic anions

Acta Crystallographica Section B Structural Science Crystal Engineering and Materials ◽

10.1107/s2052520614021428 ◽

2014 ◽

Vol 70 (6) ◽

pp. 1006-1019 ◽

Cited By ~ 1

Author(s):

Jin-Long ◽

Kazuhiro Uemura ◽

Masahiro Ebihara

Keyword(s):

Hydrogen Bonding ◽

Three Dimensional ◽

Inorganic Anions ◽

Dimensional Structure ◽

Two Dimensional ◽

Discrete Structure ◽

Torsion Angles ◽

One Dimensional ◽

Three Dimensional Structure ◽

Dirhodium Complexes

Eight new structures of dirhodium complexes, each with four biimidazole (H2bim) ligands, were obtained: [Rh2(H2bim)4(H2O)2](NO3)4·4H2O (I), [Rh2(H2bim)4(H2O)2](ClO4)4·5H2O (II), [Rh2(H2bim)4(MeOH)2](ClO4)4(III), [Rh2(H2bim)4(DMF)2](BF4)4(IV), [Rh2(H2bim)4(Mepy)2](SiF6)2·8H2O (V), [{Rh2(H2bim)4(pz)}2(μ-pz)](SiF6)(ClO4)6·12.7H2O (VI), [{Rh2(H2bim)4(pz)}2(μ-pz)](ClO4)8·11.4H2O (VII) and [Rh2(H2bim)4(μ-pz)](SiF6)2·6H2O (VIII). The unbridged Rh—Rh bond distances range between 2.6313 (8) and 2.7052 (5) Å. The dirhodium units adopt a staggered conformation with torsion angles N—Rh—Rh—N of 37.6 (4)–48.98 (8)°. Various assembled structures were constructed by hydrogen bonding between the complexes and the anions: a discrete structure in (IV), one-dimensional structure in (II), two-dimensional structures in (I), (III), (VI), (VII) and (VIII) and a three-dimensional structure in (V).

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