Extraction of Hydrogen-Atom Positions in Polyethylene Crystal Lattice from Wide-Angle Neutron Diffraction Data Collected by a Two-Dimensional Imaging Plate System:  Comparison with the X-ray and Electron Diffraction Results

2004 ◽  
Vol 37 (11) ◽  
pp. 4109-4117 ◽  
Author(s):  
Kohji Tashiro ◽  
Ichiro Tanaka ◽  
Takashi Oohara ◽  
Nobuo Niimura ◽  
Satoru Fujiwara ◽  
...  
Keyword(s):  
Hydrogen Atom ◽  
Electron Diffraction ◽  
Neutron Diffraction ◽  
Diffraction Data ◽  
Imaging Plate ◽  
Wide Angle ◽  
Two Dimensional ◽  
Neutron Diffraction Data ◽  
X Ray ◽  
Plate System

Design of a novel Peltier-based cooling device and its use in neutron diffraction data collection of perdeuterated yeast pyrophosphatase

2010 ◽  
Vol 43 (5) ◽  
pp. 1113-1120 ◽  
Author(s):  
Esko Oksanen ◽  
François Dauvergne ◽  
Adrian Goldman ◽  
Monika Budayova-Spano
Keyword(s):  
Data Collection ◽  
Neutron Diffraction ◽  
Diffraction Data ◽  
Catalytic Mechanism ◽  
Inorganic Pyrophosphatase ◽  
Neutron Diffraction Data ◽  
Cooling Device ◽  
Data Set ◽  
X Ray ◽  
X Ray Crystallography

H atoms play a central role in enzymatic mechanisms, but H-atom positions cannot generally be determined by X-ray crystallography. Neutron crystallography, on the other hand, can be used to determine H-atom positions but it is experimentally very challenging. Yeast inorganic pyrophosphatase (PPase) is an essential enzyme that has been studied extensively by X-ray crystallography, yet the details of the catalytic mechanism remain incompletely understood. The temperature instability of PPase crystals has in the past prevented the collection of a neutron diffraction data set. This paper reports how the crystal growth has been optimized in temperature-controlled conditions. To stabilize the crystals during neutron data collection a Peltier cooling device that minimizes the temperature gradient along the capillary has been developed. This device allowed the collection of a full neutron diffraction data set.

Molecular Motion in Crystalline Naphthalene:  Analysis of Multi-Temperature X-Ray and Neutron Diffraction Data

2006 ◽  
Vol 110 (41) ◽  
pp. 11695-11703 ◽  
Author(s):  
Silvia C. Capelli ◽  
Alberto Albinati ◽  
Sax A. Mason ◽  
Bertram T. M. Willis
Keyword(s):  
Neutron Diffraction ◽  
Diffraction Data ◽  
Molecular Motion ◽  
Neutron Diffraction Data ◽  
X Ray

scholarly journals Glycyl-L-alanine: a multi-temperature neutron study

2014 ◽  
Vol 70 (10) ◽  
pp. 949-952 ◽  
Author(s):  
Silvia C. Capelli ◽  
Hans-Beat Bürgi ◽  
Sax A. Mason ◽  
Dylan Jayatilaka
Keyword(s):  
Hydrogen Bonding ◽  
Neutron Diffraction ◽  
Diffraction Data ◽  
Neutron Diffraction Data ◽  
X Ray Diffraction ◽  
X Ray ◽  
Hydrogen Bonding Interactions ◽  
Anisotropic Displacement Parameters

Neutron diffraction data have been collected at 12, 50, 150 and 295 K for the dipeptide glycyl-L-alanine, C5H10N2O3, in order to obtain accurate positional and anisotropic displacement parameters for the H atoms. The values of these parameters serve as a benchmark for assessing the equivalent parameters obtained from a so-called Hirshfeld-atom refinement of X-ray diffraction data described elsewhere [Capelliet al.(2014).IUCrJ,1, 361–379]. The flexibility of the glycyl-L-alanine molecule in the solid and the hydrogen-bonding interactions as a function of temperature are also considered.

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