Mechanism of formation of lysozyme crystals in concentrated ammonium sulfate solution from concentration profiles and equilibria: Influence of the 2nd osmotic virial coefficient

被引：2

作者：

Espitalier, F.

Cheng, Y. C. ^{[1
]}

Lenhoff, A. M. ^{[1
]}

机构：

[1] Univ Delaware, Newark, DE 19716 USA

来源：

POWDER TECHNOLOGY | 2009年 / 190卷 / 1-2期

关键词：

Moment of population; Protein; Crystallization; Second virial coefficient; PROTEIN CRYSTAL; GROWTH; NUCLEATION; MOLECULES;

D O I：

10.1016/j.powtec.2008.04.085

中图分类号：

TQ [化学工业];

学科分类号：

0817 ;

摘要：

We have modelled the nucleation of the orthorhombic crystal form of lysozyme and subsequent crystal growth from concentration profiles established during the measurement of equilibrium in concentrated solutions of ammonium sulphate. A BCF mechanism for the crystal growth has been assumed. The second osmotic virial coefficient is used to calculate the activity coefficient of the protein in solution. A steep decrease of B(22) is predicted for salt molalities higher than 6.8 m. (C) 2008 Elsevier B.V. All rights reserved.

引用

页码：112 / 117

页数：6

共 9 条

[1] Hydration, mobility and accessibility of lysozyme: structures of a pH 6.5 orthorhombic form and its low-humidity variant and a comparative study involving 20 crystallographically independent molecules [J].