Characterization of dislocations in protein crystals by means of synchrotron double-crystal topography

被引：21

作者：

Capelle, B

Epelboin, Y

Härtwig, J

Moraleda, AB

Otálora, F

Stojanoff, V

机构：

[1] Univ Paris 06, CNRS, UMR 7590, LMCP, F-75252 Paris, France

[2] European Synchrotron Radiat Facil, F-38043 Grenoble, France

[3] LEC, IACT, Fac Ciencias, Granada 18002, Spain

[4] Brookhaven Natl Lab, Natl Synchrotron Light Source, Upton, NY 11973 USA

来源：

JOURNAL OF APPLIED CRYSTALLOGRAPHY | 2004年 / 37卷

关键词：

D O I：

10.1107/S0021889803024415

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Hen egg-white lysozyme (HEWL) crystals have been studied by means of double-crystal synchrotron topography. The crystals reveal a number of features that are quite well known in hydrothermally grown inorganic crystals: dislocations, growth bands and growth sector boundaries. Dislocations in the (110) sectors have been characterized as edge dislocations with Burgers vector parallel to the c axis. They are distinguishable only under weak beam conditions. The presence of edge dislocations shown in this paper is consistent with the spiral growth steps previously reported. This spiral growth on protein crystals has been observed many times by surface techniques.

引用

页码：67 / 71

页数：5

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