PACKING FORCES IN RIBONUCLEASE CRYSTALS

被引：7

作者：

CROSIO, MP

RODIER, F

JULLIEN, M

机构：

[1] Laboratoire de Biologie physico-chimique, Université Paris Sud, Orsay

来源：

FEBS LETTERS | 1990年 / 271卷 / 1-2期

关键词：

Buried surface area; Crystal packing; Ribonuclease A; Ribonuclease S;

D O I：

10.1016/0014-5793(90)80395-Y

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Packing in Ribonuclease A and Ribonuclease S crystals have been compared in order to determine the possible role of the precipitant on lattice contacts. Both proteins have similar tertiary structures, buth they crystallize in different space groups depending on the precipitating agent. It is found that packing differs either by the number of nearest neighbours or by the size of surface areas buried in individual contacts. Ammonium sulfate seems to promote hydrophobic interactions with interfaces similar to those found in oligomeric proteins. Organic precipitants favour electrostatic interactions. © 1990.

引用

页码：152 / 156

页数：5

共 23 条

[1] RIBONUCLEASE-A - LEAST-SQUARES REFINEMENT OF THE STRUCTURE AT 1.45 A RESOLUTION [J].