The Solubility of Orthorhombic Lysozyme Crystals Obtained at High pH

被引:46
作者
Aldabaibeh, Naser [1 ,2 ]
Jones, Matthew J. [1 ]
Myerson, Allan S. [2 ]
Ulrich, Joachim [1 ]
机构
[1] Univ Halle Wittenberg, Zentrum Ingn Wissensch, Verfahrenstech TVT, D-06099 Halle, Saale, Germany
[2] IIT, Dept Biol & Chem Engn, Chicago, IL 60616 USA
基金
美国国家卫生研究院;
关键词
EGG-WHITE LYSOZYME; CRYSTALLIZATION; PROTEIN; TEMPERATURE; GROWTH; POLYMORPHISM; MECHANISMS; MOLECULES;
D O I
10.1021/cg900113e
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
The high pH region of the phase diagram of lysozyme with NaCl as a precipitant was determined. In this region of the phase diagram, lysozyme crystallizes in one of two different orthorhombic modifications, the low and high temperature orthorhombic modifications. The solubility of two modifications was measured at different temperatures, pH values, and NaCl concentrations. Both modifications show a similar dependence on the solution conditions where solubility increases with temperature and decreases with pH and NaCl concentration. The transition temperature between the two modifications was determined from the solubility curves and was shown to increase with pH and NaCl concentration. At pH values close to the isoelectric point (pH 11), the transition temperature becomes independent of NaCl concentration.
引用
收藏
页码:3313 / 3317
页数:5
相关论文
共 30 条
[1]   Solubility of thaumatin [J].
Asherie, Neer ;
Ginsberg, Charles ;
Blass, Samuel ;
Greenbaum, Arieh ;
Knafo, Sarah .
CRYSTAL GROWTH & DESIGN, 2008, 8 (06) :1815-1817
[2]   Thermodynamics of the hydrophobicity in crystallization of insulin [J].
Bergeron, L ;
Filobelo, LF ;
Galkin, O ;
Vekilov, PG .
BIOPHYSICAL JOURNAL, 2003, 85 (06) :3935-3942
[3]   The Protein Data Bank [J].
Berman, HM ;
Westbrook, J ;
Feng, Z ;
Gilliland, G ;
Bhat, TN ;
Weissig, H ;
Shindyalov, IN ;
Bourne, PE .
NUCLEIC ACIDS RESEARCH, 2000, 28 (01) :235-242
[4]   INFLUENCE OF UREA ON CRYSTALLIZATION AND POLYMORPHISM OF HEN LYSOZYME [J].
BERTHOU, J ;
JOLLES, P .
FEBS LETTERS, 1973, 31 (02) :189-192
[5]   Multiple extrema in the intermolecular potential and the phase diagram of protein solutions [J].
Brandon, Simon ;
Katsonis, Panagiotis ;
Vekilov, Peter G. .
PHYSICAL REVIEW E, 2006, 73 (06)
[6]   THE SOLUBILITY OF THE TETRAGONAL FORM OF HEN EGG-WHITE LYSOZYME FROM PH 4.0 TO 5.4 [J].
CACIOPPO, E ;
PUSEY, ML .
JOURNAL OF CRYSTAL GROWTH, 1991, 114 (03) :286-292
[7]   Hydrophobic forces between protein molecules in aqueous solutions of concentrated electrolyte [J].
Curtis, RA ;
Steinbrecher, C ;
Heinemann, A ;
Blanch, HW ;
Prausnitz, JM .
BIOPHYSICAL CHEMISTRY, 2002, 98 (03) :249-265
[8]   Estimating lysozyme crystallization growth rates and solubility from isothermal microcalorimetry [J].
Darcy, PA ;
Wiencek, JM .
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 1998, 54 :1387-1394
[9]   THE SOLUBILITY DEPENDENCE OF CANAVALIN ON PH AND TEMPERATURE [J].
DEMATTEI, RC ;
FEIGELSON, RS .
JOURNAL OF CRYSTAL GROWTH, 1991, 110 (1-2) :34-40
[10]   KINETIC-STUDIES ON THE GROWTH OF 3 CRYSTAL FORMS OF LYSOZYME BASED ON THE MEASUREMENT OF PROTEIN AND CL- CONCENTRATION CHANGES [J].
ELGERSMA, AV ;
ATAKA, M ;
KATSURA, T .
JOURNAL OF CRYSTAL GROWTH, 1992, 122 (1-4) :31-40