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Design of a novel Peltier‐based cooling device and its use in neutron diffraction data collection of perdeuterated yeast pyrophosphatase
Author(s) -
Oksanen Esko,
Dauvergne François,
Goldman Adrian,
BudayovaSpano Monika
Publication year - 2010
Publication title -
journal of applied crystallography
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.429
H-Index - 162
ISSN - 1600-5767
DOI - 10.1107/s0021889810027111
Subject(s) - neutron diffraction , crystallography , materials science , neutron , inorganic pyrophosphatase , diffraction , thermoelectric effect , resolution (logic) , yeast , chemistry , crystal structure , enzyme , optics , physics , thermodynamics , organic chemistry , nuclear physics , computer science , biochemistry , artificial intelligence , pyrophosphate
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.