Systematic Investigations of the Dipolar Interaction in Aromatic Liquids. A Neutron Diffraction Experiment I. Structure Factors and Intramolecular Structure

1988 ◽  
Vol 92 (10) ◽  
pp. 1149-1158 ◽  
Author(s):  
H. Bertagnolli ◽  
I. Hummel ◽  
P. Chieux
1985 ◽  
Vol 40 (2) ◽  
pp. 191-192
Author(s):  
A. Wildermuth ◽  
P. Lamparter ◽  
S. Steeb

By neutron diffraction using the method of isotopic substitution with the amorphous alloy Ni31Dy69 the partial structure factors SNiNi, SDyDy and SNiDy were obtained, furthermore with the same specimen containing 10 a/o deuterium a partial structure factor SDD resulted. For the evaluation of SDD it was necessary to perform the neutron diffraction experiment with an alloy whose both components were zero scattering isotopic mixtures of Ni or Dy, respectively.


1982 ◽  
Vol 37 (11) ◽  
pp. 1215-1222
Author(s):  
F. Paasche ◽  
H. Olbrich ◽  
G. Rainer-Harbach ◽  
P. Lamparter ◽  
S. Steeb

Electron diffraction with amorphous Fe80B20 and Mn73Si27 yields structure factors and pair correlation functions which are discussed together with the results of X-ray- and neutron-diffraction experiments. For Mn73Si27 additional interesting details are revealed. A tetrahedral model for Mn73Si27 is described. Finally we show that the evaluation of partial structure factors by the three beam experiment, i.e. the combination of an electron-, X-ray- and neutron-diffraction experiment is not possible in general.


1987 ◽  
Vol 87 (4) ◽  
pp. 2278-2281 ◽  
Author(s):  
Marie‐Louise Saboungi ◽  
R. Blomquist ◽  
K. J. Volin ◽  
D. L. Price

2020 ◽  
Vol 76 (11) ◽  
pp. 1050-1056
Author(s):  
Katsuhiro Kusaka ◽  
Takeshi Yokoyama ◽  
Taro Yamada ◽  
Naomine Yano ◽  
Ichiro Tanaka ◽  
...  

Transthyretin (TTR) is one of more than 30 amyloidogenic proteins, and the amyloid fibrils found in patients afflicted with ATTR amyloidosis are composed of this protein. Wild-type TTR amyloids accumulate in the heart in senile systemic amyloidosis (SSA). ATTR amyloidosis occurs at a much younger age than SSA, and the affected individuals carry a TTR mutant. The naturally occurring amyloidogenic Y116S TTR variant forms more amyloid fibrils than wild-type TTR. Thus, the Y116S mutation reduces the stability of the TTR structure. A neutron diffraction experiment on Y116S TTR was performed to elucidate the mechanism of the changes in structural stability between Y116S variant and wild-type TTR through structural comparison. Large crystals of the Y116S variant were grown under optimal crystallization conditions, and a single 2.4 mm3 crystal was ultimately obtained. This crystal was subjected to time-of-flight (TOF) neutron diffraction using the IBARAKI biological crystal diffractometer (iBIX) at the Japan Proton Accelerator Research Complex, Tokai, Japan (J-PARC). A full data set for neutron structure analysis was obtained in 14 days at an operational accelerator power of 500 kW. A new integration method was developed and showed improved data statistics; the new method was applied to the reduction of the TOF diffraction data from the Y116S variant. Data reduction was completed and the integrated intensities of the Bragg reflections were obtained at 1.9 Å resolution for structure refinement. Moreover, X-ray diffraction data at 1.4 Å resolution were obtained for joint neutron–X-ray refinement.


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