Design of a novel Peltier-based cooling device and its use in neutron diffraction data collection of perdeuterated yeast pyrophosphatase
作者： Esko Oksanen , François Dauvergne , Adrian Goldman , Monika Budayova-Spano
DOI: 10.1107/S0021889810027111
关键词:
摘要: 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 used to determine it is experimentally very challenging. Yeast inorganic pyrophosphatase (PPase) an essential enzyme that has been studied extensively yet details of catalytic mechanism remain incompletely understood. The temperature instability PPase crystals past prevented collection neutron diffraction data set. This paper reports how crystal growth optimized temperature-controlled conditions. To stabilize during Peltier cooling device minimizes gradient along capillary developed. allowed full
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