scholarly journals Crystal structure of a Vip3B family insecticidal protein reveals a new fold and a unique tetrameric assembly

2019 ◽  
Vol 29 (4) ◽  
pp. 824-829 ◽  
Author(s):  
Meiying Zheng ◽  
Artem G. Evdokimov ◽  
Farhad Moshiri ◽  
Casey Lowder ◽  
Jeff Haas
Keyword(s):  
Crystal Structure ◽  
Insecticidal Protein ◽  
Tetrameric Assembly

High pressure macromolecular crystallography: The 140-MPa crystal structure at 2.3 Å resolution of urate oxidase, a 135-kDa tetrameric assembly

2006 ◽  
Vol 1764 (3) ◽  
pp. 391-397 ◽  
Author(s):  
Nathalie Colloc'h ◽  
Eric Girard ◽  
Anne-Claire Dhaussy ◽  
Richard Kahn ◽  
Isabella Ascone ◽  
...  
Keyword(s):  
Crystal Structure ◽  
High Pressure ◽  
Urate Oxidase ◽  
Macromolecular Crystallography ◽  
Tetrameric Assembly

scholarly journals Crystal structure of a β-aminopeptidase from an AustralianBurkholderiasp.

2017 ◽  
Vol 73 (7) ◽  
pp. 386-392 ◽  
Author(s):  
Marietta John-White ◽  
Geoff J. Dumsday ◽  
Priscilla Johanesen ◽  
Dena Lyras ◽  
Nyssa Drinkwater ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Amino Acids ◽  
Wastewater Treatment ◽  
Mechanism Of Action ◽  
Treatment Plant ◽  
Β Subunit ◽  
Α Subunit ◽  
Gram Negative ◽  
X Ray ◽  
Tetrameric Assembly

β-Aminopeptidases are a unique group of enzymes that have the unusual capability to hydrolyze N-terminal β-amino acids from synthetic β-peptides. β-Peptides can form secondary structures mimicking α-peptide-like structures that are resistant to degradation by most known proteases and peptidases. These characteristics of β-peptides give them great potential as peptidomimetics. Here, the X-ray crystal structure of BcA5-BapA, a β-aminopeptidase from a Gram-negativeBurkholderiasp. that was isolated from activated sludge from a wastewater-treatment plant in Australia, is reported. The crystal structure of BcA5-BapA was determined to a resolution of 2.0 Å and showed a tetrameric assembly typical of the β-aminopeptidases. Each monomer consists of an α-subunit (residues 1–238) and a β-subunit (residues 239–367). Comparison of the structure of BcA5-BapA with those of other known β-aminopeptidases shows a highly conserved structure and suggests a similar proteolytic mechanism of action.

scholarly journals The crystal structure of haemoglobin from Atlantic cod

2019 ◽  
Vol 75 (8) ◽  
pp. 537-542
Author(s):  
Ronny Helland ◽  
Eva Katrin Bjørkeng ◽  
Ulli Rothweiler ◽  
Magne Olav Sydnes ◽  
Daniela Maria Pampanin
Keyword(s):  
Crystal Structure ◽  
Atlantic Cod ◽  
Asymmetric Unit ◽  
Tetrameric Assembly

The crystal structure of haemoglobin from Atlantic cod has been solved to 2.54 Å resolution. The structure consists of two tetramers in the crystallographic asymmetric unit. The structure of haemoglobin obtained from one individual cod suggests polymorphism in the tetrameric assembly.

scholarly journals Structural Basis for Interaction Between NO66 and Osterix

2014 ◽  
Vol 70 (a1) ◽  
pp. C313-C313
Author(s):  
Minhao Wu ◽  
Yue Tao ◽  
Xing Zhou ◽  
Krishna Sinha ◽  
Jianye Zang
Keyword(s):  
Crystal Structure ◽  
Bone Formation ◽  
Osteoblast Differentiation ◽  
Critical Role ◽  
Transcriptional Factor ◽  
Structural Basis ◽  
Regulation Network ◽  
Jmjc Domain ◽  
Tetrameric Assembly ◽  
Hinge Domain

The differentiation of mesenchymal stem cells to osteoblasts is one of the critical steps of bone formation. Osterix (Osx) is an osteoblast-specific transcriptional factor required for bone formation and osteoblast differentiation, which has been shown to interact with other factors to control the expression of osteoblast-specific genes. A novel JmjC domain containing protein NO66 has been identified in the regulation network of Osx, which plays an important role in osteoblast differentiation through interaction with Osx. Here we report the crystal structure of NO66, showing it exists as a functional tetramer form. A hinge domain links N-terminal JmjC domain and C-terminal wHTH domain of NO66 and is essential for its tetrameric assembly. The oligomerization interface of NO66 provides the binding site for Osx, which interacts with a conserved fragment of Osx. Further work demonstrates that the hinge domain-dependent oligomerization is essential for NO66 to interact with Osx and controls Osx-dependent gene expression. Our finding reveals that homo-oligomerization of JmjC domain containing proteins plays a critical role in interaction with regulatory factors and may have significant physiological roles.

scholarly journals Structure of human collapsin response mediator protein 1: a possible role of its C-terminal tail

2015 ◽  
Vol 71 (8) ◽  
pp. 938-945 ◽  
Author(s):  
Szu-Heng Liu ◽  
Shih-Fang Huang ◽  
Yuan-Ling Hsu ◽  
Szu-Hua Pan ◽  
Yen-Ju Chen ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Structural Changes ◽  
Collapsin Response Mediator Protein ◽  
Mediator Protein ◽  
Dynamics And Function ◽  
And Function ◽  
Tetrameric Assembly

Collapsin response mediator protein 1 (CRMP-1) is the first identified member of the CRMP family and is crucial for both the mediation of neuronal differentiation and in suppressing the invasion of lung cancer. The crystal structure of full-length human CRMP-1 was determined at a resolution of 3 Å. Human CRMP-1 comprises a tetrameric assembly; its overall structure is similar to that of mouse CRMP-1, but the measured electron density of the C-terminal residues 488–496 show a randomly coiled link that connects the protomers to each other, within which residues 497–572 are proteolytically susceptiblein vivo. Deletion of residues 472–572 by thrombinin vitronot only releases a randomly coiled tail but also transduces observable structural changes of CRMP-1, as revealed by analytical size-exclusive chromatography and circular dichroism spectra. These results indicate a possible alternative role in CRMP dynamics and function.

Crystal Structure Determination of Glycerol-Containing Lipids from Electron Diffraction Data. Use of Analog Compounds Based upon Configurational Isomers of Cyclopentane-1, 2, 3-TRIOL

1977 ◽  
Vol 35 ◽  
pp. 24-25
Author(s):  
Douglas L. Dorset ◽  
Anthony J. Hancock
Keyword(s):  
Crystal Structure ◽  
Electron Diffraction ◽  
Diffraction Data ◽  
Structure Determination ◽  
Crystal Surface ◽  
Coherent Scattering ◽  
Crystal Structure Determination ◽  
Electron Diffraction Data ◽  
Polar Group ◽  
Axis Orientation

Lipids containing long polymethylene chains were among the first compounds subjected to electron diffraction structure analysis. It was only recently realized, however, that various distortions of thin lipid microcrystal plates, e.g. bends, polar group and methyl end plane disorders, etc. (1-3), restrict coherent scattering to the methylene subcell alone, particularly if undistorted molecular layers have well-defined end planes. Thus, ab initio crystal structure determination on a given single uncharacterized natural lipid using electron diffraction data can only hope to identify the subcell packing and the chain axis orientation with respect to the crystal surface. In lipids based on glycerol, for example, conformations of long chains and polar groups about the C-C bonds of this moiety still would remain unknown.One possible means of surmounting this difficulty is to investigate structural analogs of the material of interest in conjunction with the natural compound itself. Suitable analogs to the glycerol lipids are compounds based on the three configurational isomers of cyclopentane-1,2,3-triol shown in Fig. 1, in which three rotameric forms of the natural glycerol derivatives are fixed by the ring structure (4-7).

Spherulitic crystal growth in the prodissoconch larval of Crassostrea virginica

1983 ◽  
Vol 41 ◽  
pp. 518-519
Author(s):  
George G. Cocks ◽  
Louis Leibovitz ◽  
DoSuk D. Lee
Keyword(s):  
Crystal Structure ◽  
Crassostrea Virginica ◽  
Crystal Orientation ◽  
Developmental Changes ◽  
Gastrula Stage ◽  
Orthorhombic Crystal ◽  
Orthorhombic Crystal Structure ◽  
Stages Of Growth ◽  
Early Stages ◽  
Initial Deposition

Our understanding of the structure and the formation of inorganic minerals in the bivalve shells has been considerably advanced by the use of electron microscope. However, very little is known about the ultrastructure of valves in the larval stage of the oysters. The present study examines the developmental changes which occur between the time of conception to the early stages of Dissoconch in the Crassostrea virginica(Gmelin), focusing on the initial deposition of inorganic crystals by the oysters.The spawning was induced by elevating the temperature of the seawater where the adult oysters were conditioned. The eggs and sperm were collected separately, then immediately mixed for the fertilizations to occur. Fertilized animals were kept in the incubator where various stages of development were stopped and observed. The detailed analysis of the early stages of growth showed that CaCO3 crystals(aragonite), with orthorhombic crystal structure, are deposited as early as gastrula stage(Figuresla-b). The next stage in development, the prodissoconch, revealed that the crystal orientation is in the form of spherulites.

Transmission Electron Microscopy studies of the vacancy ordering in YSI2-X thin films

1991 ◽  
Vol 49 ◽  
pp. 562-563
Author(s):  
F.-R. Chen ◽  
T. L. Lee ◽  
L. J. Chen
Keyword(s):  
Crystal Structure ◽  
Electron Microscopy ◽  
Thin Films ◽  
Diffraction Pattern ◽  
Annealing Temperature ◽  
Lattice Mismatch ◽  
Si Substrate ◽  
Metal Thin Films ◽  
Transmission Electron ◽  
Vacancy Ordering

YSi2-x thin films were grown by depositing the yttrium metal thin films on (111)Si substrate followed by a rapid thermal annealing (RTA) at 450 to 1100°C. The x value of the YSi2-x films ranges from 0 to 0.3. The (0001) plane of the YSi2-x films have an ideal zero lattice mismatch relative to (111)Si surface lattice. The YSi2 has the hexagonal AlB2 crystal structure. The orientation relationship with Si was determined from the diffraction pattern shown in figure 1(a) to be and . The diffraction pattern in figure 1(a) was taken from a specimen annealed at 500°C for 15 second. As the annealing temperature was increased to 600°C, superlattice diffraction spots appear at position as seen in figure 1(b) which may be due to vacancy ordering in the YSi2-x films. The ordered vacancies in YSi2-x form a mesh in Si plane suggested by a LEED experiment.

Crystal Structure Analysis of Cu-Zr Alloys by Convergent Beam Diffraction

1981 ◽  
Vol 39 ◽  
pp. 354-355
Author(s):  
A. F. Marshall ◽  
J. W. Steeds ◽  
D. Bouchet ◽  
S. L. Shinde ◽  
R. G. Walmsley
Keyword(s):  
Crystal Structure ◽  
Point Group ◽  
Intermetallic Phase ◽  
Three Dimensional ◽  
Crystal Structure Analysis ◽  
Ion Milling ◽  
Composition And Structure ◽  
Unit Cells ◽  
Sputter Deposited ◽  
Convergent Beam

Convergent beam electron diffraction is a powerful technique for determining the crystal structure of a material in TEM. In this paper we have applied it to the study of the intermetallic phases in the Cu-rich end of the Cu-Zr system. These phases are highly ordered. Their composition and structure has been previously studied by microprobe and x-ray diffraction with sometimes conflicting results.The crystalline phases were obtained by annealing amorphous sputter-deposited Cu-Zr. Specimens were thinned for TEM by ion milling and observed in a Philips EM 400. Due to the large unit cells involved, a small convergence angle of diffraction was used; however, the three-dimensional lattice and symmetry information of convergent beam microdiffraction patterns is still present. The results are as follows:1) 21 at% Zr in Cu: annealed at 500°C for 5 hours. An intermetallic phase, Cu3.6Zr (21.7% Zr), space group P6/m has been proposed near this composition (2). The major phase of our annealed material was hexagonal with a point group determined as 6/m.

High resolution STEM imaging study on high Tc superconductor YBa2CuaO7-x

1988 ◽  
Vol 46 ◽  
pp. 882-883
Author(s):  
H.-J. Ou ◽  
J. M. Cowley
Keyword(s):  
Crystal Structure ◽  
High Resolution ◽  
Grain Boundary ◽  
Strong Field ◽  
Imaging Study ◽  
Structure Defects ◽  
High Tc ◽  
High Tc Superconductor ◽  
Diffraction Patterns ◽  
Lattice Planes

Using the dedicate VG-HB5 STEM microscope, the crystal structure of high Tc superconductor of YBa2Cu3O7-x has been studied via high resolution STEM (HRSTEM) imaging and nanobeam (∽3A) diffraction patterns. Figure 1(a) and 2(a) illustrate the HRSTEM image taken at 10' times magnification along [001] direction and [100] direction, respectively. In figure 1(a), a grain boundary with strong field contrast is seen between two crystal regions A and B. The grain boundary appears to be parallel to a (110) plane, although it is not possible to determine [100] and [001] axes as it is in other regions which contain twin planes [3]. Following the horizontal lattice lines, from left to right across the grain boundary, a lattice bending of ∽4° is noticed. Three extra lattice planes, indicated by arrows, were found to terminate at the grain boundary and form dislocations. It is believed that due to different chemical composition, such structure defects occur during crystal growth. No bending is observed along the vertical lattice lines.

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