Slow cooling and temperature-controlled protein crystallography.
Slow cooling and temperature-controlled protein crystallography.
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DOI：
10.1007/s10969-009-9074-y
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发表时间：
2010-03
期刊：
影响因子：
--
通讯作者：
Thorne, Robert E
中科院分区：
文献类型：
--
作者：
Warkentin, Matthew;Thorne, Robert E
在晶体学中，样品的快速冷却通常被认为是防止溶剂结晶和相关的样品损坏所必需的。结果表明，在不添加穿透性冷冻保护剂的情况下，许多蛋白质晶体可以在0.1K/S的温度下成功地冷却到T=100K。当闪冷失效时，慢速冷却提供了另一种选择，可以在T=300K到T=100K的所有温度下对蛋白质的结构和功能进行衍射研究。
In cryocrystallography, rapid sample cooling is generally deemed essential to prevent solvent crystallization and associated sample damage. We show that by carefully and completely removing all external solvent, many protein crystals can be successfully cooled to T=100 K at only 0.1 K/s without additional penetrating cryoprotectants. Slow cooling provides an alternative when flash cooling fails, and enables diffraction studies of protein structure and function at all temperatures between T=300 K and T=100 K.