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Cryoprotectant‐free high‐pressure cooling and dynamic nuclear polarization for more sensitive detection of hydrogen in neutron protein crystallography

机译:冷却和冷冻保护剂还是免费的高压力动态核极化更敏感在中子检测氢蛋白质晶体学

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摘要

To improve the sensitivity of hydrogen detection using neutrons, a proton‐polarization technique together with a high‐pressure cooling method is necessary. The highest pressure (200?MPa) used in the experiment described here enabled relatively large protein crystals to be cooled without any cryoprotectants while retaining the protein structure, and it was confirmed that high‐pressure‐cooled crystals diffracted to nearly the same resolution as flash‐cooled small crystals soaked with cryoprotectants. Dynamic nuclear polarization was used as a proton‐polarization technique for protein crystals, and ~300?mg polycrystalline protein doped with TEMPOL gave a maximum proton polarization of 22.3% at a temperature of 0.5?K in a 2.5?T magnetic field.
机译:提高氢检测的敏感性使用中子,质子极化技术加上高压力冷却方法必要的。这里所描述的实验使相对大的蛋白质晶体没有冷却冷冻保护剂,同时保持蛋白质结构,这是证实高压力检测冷却晶体衍射几乎相同的分辨率flash冷却小晶体浸泡冷冻保护剂。核极化被用作质子的极化技术对蛋白质晶体,~ 300 ?掺杂TEMPOL最大质子22.3%的极化温度为0.5 ?在2.5 ?

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