Importance of the nature of anions in lysozyme crystallisation correlated with protein net charge variation

被引:43
作者
Retailleau, P
Ducruix, A
Riès-Kautt, M
机构
[1] Univ Paris 05, Fac Pharm, UMR 8015, Lab Cristallog & RMN Biol, F-75270 Paris 06, France
[2] Ctr Univ Paris Sud, Lab LURE, F-91898 Orsay, France
来源
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2002年 / 58卷
关键词
lysozyme; crystallisation; solubility; Hofmeister series; electrostatic effects; polyelectrolytes; anions;
D O I
10.1107/S0907444902014592
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Hofmeister anion series are studied to examine the coupled influence of pH and ionic strength on the solubility of previously desalted lysozyme. Solubility curves are measured at pH 4.3 and 8. 3 and 18degrees C for nitrate, para-toluenesulfonate, citrate, sulphate, phosphate, and acetate. Extreme low ionic strength is explored, confirming the decrease of lysozyme solubility while increasing the protein net charge and the ionic strength. The classification of specific salt effects takes into account the valence of the anions with respect to the protein net charge.
引用
收藏
页码:1576 / 1581
页数:6
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