Structural characterization of ultrathin cuprate artificial superconducting structures by x-ray synchrotron radiation

2003 ◽  
Vol 94 (10) ◽  
pp. 6991-6993 ◽  
Author(s):  
C. Aruta ◽  
M. Angeloni ◽  
G. Balestrino ◽  
P. G. Medaglia ◽  
P. Orgiani ◽  
...  
1996 ◽  
Vol 49 (12) ◽  
pp. 1273 ◽  
Author(s):  
AL Maclean ◽  
GJ Foran ◽  
BJ Kennedy ◽  
P Turner ◽  
TW Hambley

The structure of 5,10,15,20-tetraphenylporphinatonickel(II) ([Ni( tpp )]) has been studied by both X-ray diffraction (powder and single-crystal methods) and EXAFS. The bond lengths obtained from analysis of the EXAFS agree, within standard deviations, with those obtained from the X-ray diffraction studies. The Ni-N bond length of 1.93(1) Ǻ agrees especially well with the value of 1.931(2) Ǻ obtained from the single-crystal analysis. The powder X-ray diffraction pattern, collected by using synchrotron radiation, is presented.


2017 ◽  
Vol 13 ◽  
pp. 1145-1167 ◽  
Author(s):  
Serge Pérez ◽  
Daniele de Sanctis

Synchrotron radiation is the most versatile way to explore biological materials in different states: monocrystalline, polycrystalline, solution, colloids and multiscale architectures. Steady improvements in instrumentation have made synchrotrons the most flexible intense X-ray source. The wide range of applications of synchrotron radiation is commensurate with the structural diversity and complexity of the molecules and macromolecules that form the collection of substrates investigated by glycoscience. The present review illustrates how synchrotron-based experiments have contributed to our understanding in the field of structural glycobiology. Structural characterization of protein–carbohydrate interactions of the families of most glycan-interacting proteins (including glycosyl transferases and hydrolases, lectins, antibodies and GAG-binding proteins) are presented. Examples concerned with glycolipids and colloids are also covered as well as some dealing with the structures and multiscale architectures of polysaccharides. Insights into the kinetics of catalytic events observed in the crystalline state are also presented as well as some aspects of structure determination of protein in solution.


1999 ◽  
Vol 183 (2) ◽  
pp. 222-231 ◽  
Author(s):  
C. Lamberti ◽  
S. Bordiga ◽  
A. Zecchina ◽  
A. Carati ◽  
A.N. Fitch ◽  
...  

2007 ◽  
Vol 2007 (suppl_26) ◽  
pp. 61-66 ◽  
Author(s):  
B. Peplinski ◽  
B. Adamczyk ◽  
G. Kley ◽  
K. Adam ◽  
F. Emmerling ◽  
...  

Author(s):  
Shabana Noor ◽  
Richard Goddard ◽  
Fehmeeda Khatoon ◽  
Sarvendra Kumar ◽  
Rüdiger W. Seidel

AbstractSynthesis and structural characterization of two heterodinuclear ZnII-LnIII complexes with the formula [ZnLn(HL)(µ-OAc)(NO3)2(H2O)x(MeOH)1-x]NO3 · n H2O · n MeOH [Ln = Pr (1), Nd (2)] and the crystal and molecular structure of [ZnNd(HL)(µ-OAc)(NO3)2(H2O)] [ZnNd(HL)(OAc)(NO3)2(H2O)](NO3)2 · n H2O · n MeOH (3) are reported. The asymmetrical compartmental ligand (E)-2-(1-(2-((2-hydroxy-3-methoxybenzylidene)amino)-ethyl)imidazolidin-2-yl)-6-methoxyphenol (H2L) is formed from N1,N3-bis(3-methoxysalicylidene)diethylenetriamine (H2valdien) through intramolecular aminal formation, resulting in a peripheral imidazoline ring. The structures of 1–3 were revealed by X-ray crystallography. The smaller ZnII ion occupies the inner N2O2 compartment of the ligand, whereas the larger and more oxophilic LnIII ions are found in the outer O2O2’ site. Graphic Abstract Synthesis and structural characterization of two heterodinuclear ZnII-LnIII complexes (Ln = Pr, Nd) bearing an asymmetrical compartmental ligand formed in situ from N1,N3-bis(3-methoxysalicylidene)diethylenetriamine (H2valdien) through intramolecular aminal formation are reported.


2012 ◽  
Vol 45 (3) ◽  
pp. 307-312 ◽  
Author(s):  
Takamichi Shinohara ◽  
Tomoko Shirahase ◽  
Daiki Murakami ◽  
Taiki Hoshino ◽  
Moriya Kikuchi ◽  
...  

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