Temperature-dependent solubility of selected proteins

被引:68
|
作者
Christopher, GK
Phipps, AG
Gray, RJ
机构
[1] Diversified Sci Inc, Birmingham, AL 35211 USA
[2] Univ Alabama, Ctr Macromol Crystallog, Birmingham, AL 35294 USA
基金
美国国家航空航天局;
关键词
solubility; proteins; temperature;
D O I
10.1016/S0022-0248(98)00355-8
中图分类号
O7 [晶体学];
学科分类号
0702 ; 070205 ; 0703 ; 080501 ;
摘要
Temperature is being recognized as a noninvasive control parameter for protein crystallization. Before temperature-induced crystallization can be routinely used as a method of preparation of protein crystals, qualitative data on the temperature dependent solubility of the protein must be obtained. Qualitative data for tt temperature-dependent solubility is available for a limited number of proteins. We report herein qualitative temperature-dependent solubility data for selected proteins as obtained by the use of a multichambered thermal gradient device. These studies demonstrate that a large percentage of proteins do in fact exhibit a solubility versus temperature dependence which suggests that temperature can be used as an alternative crystallization technique for proteins. (C) 1998 Elsevier Science B.V. All rights reserved.
引用
收藏
页码:820 / 826
页数:7
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