scholarly journals The First Neptunium Dioxide Neutron Diffraction Experiment at HFIR

2021 ◽  
Author(s):  
Luke Sadergaski ◽  
Sam Schrell ◽  
Kaara Patton ◽  
Matthias Frontzek
Keyword(s):  
Neutron Diffraction ◽  
Diffraction Experiment ◽  
Neutron Diffraction Experiment ◽  
Neptunium Dioxide

Structure of liquid equiatomic potassium–lead alloy: A neutron diffraction experiment

1987 ◽  
Vol 87 (4) ◽  
pp. 2278-2281 ◽  
Author(s):  
Marie‐Louise Saboungi ◽  
R. Blomquist ◽  
K. J. Volin ◽  
D. L. Price
Keyword(s):  
Neutron Diffraction ◽  
Lead Alloy ◽  
Diffraction Experiment ◽  
Neutron Diffraction Experiment ◽  
Structure Of Liquid

Neutron diffraction experiment with the Y116S variant of transthyretin using iBIX at J-PARC: application of a new integration method

2020 ◽  
Vol 76 (11) ◽  
pp. 1050-1056
Author(s):  
Katsuhiro Kusaka ◽  
Takeshi Yokoyama ◽  
Taro Yamada ◽  
Naomine Yano ◽  
Ichiro Tanaka ◽  
...  
Keyword(s):  
Neutron Diffraction ◽  
Diffraction Data ◽  
Amyloid Fibrils ◽  
Integration Method ◽  
Proton Accelerator ◽  
Diffraction Experiment ◽  
Wild Type ◽  
Neutron Diffraction Experiment ◽  
X Ray ◽  
Attr Amyloidosis

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.

Hydration structures in proteins and neutron diffraction experiment on dissimilatory sulfite reductase D (DsrD)

2003 ◽  
Vol 11 (1) ◽  
pp. 72-75 ◽  
Author(s):  
Toshiyuki Chatake ◽  
Andreas Ostermann ◽  
Kazuo Kurihara ◽  
Fritz G. Parak ◽  
Nobuhiro Mizuno ◽  
...  
Keyword(s):  
Neutron Diffraction ◽  
Sulfite Reductase ◽  
Diffraction Experiment ◽  
Neutron Diffraction Experiment ◽  
Dissimilatory Sulfite Reductase
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