Protein crystallisation on chemically modified mica surfaces

被引：63

作者：

Falini, G ^{[1
]}

Fermani, S ^{[1
]}

Conforti, G ^{[1
]}

Ripamonti, A ^{[1
]}

机构：

[1] Univ Bologna, Dipartimento Chim G Ciamician, Alma Mater Studiorum, I-40126 Bologna, Italy

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 2002年 / 58卷

关键词：

mica; protein crystallisation; lysozyme; concanavalin A; thaumatin; heterogeneous nucleation;

D O I：

10.1107/S0907444902012763

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Chemically modified mica sheets have been tested as heterogeneous nucleant surfaces for lysozyme, concanavalin A and thaumatin. Smooth mica surfaces with reduced hydrophilic properties and different density of ionisable groups have been prepared by a silanisation reaction using mixtures of n-propyltriethoxysilane and 3-aminopropyltriethoxysilane in different percentages starting from 0 to 100% of aminosilane. The crystallisation experiments were carried out with the hanging drop vapour diffusion technique. The results suggest that these mica surfaces act as heterogeneous nucleant agents, whose effectiveness is due to non-specific attractive and local interactions between charged residues of the protein and the ionisable groups on the mica surfaces.

引用

页码：1649 / 1652

页数：4

共 18 条

[1] Is lysozyme really the ideal model protein? [J].