Measuring the elastic properties of protein crystals by brillouin scattering

被引：25

作者：

Caylor, CL

Speziale, S

Kriminski, S

Duffy, T

Zha, CS

Thorne, RE ^{[1
]}

机构：

[1] Cornell Univ, Atom & Solid State Phys Lab, Ithaca, NY 14853 USA

[2] Princeton Univ, Dept Geosci, Princeton, NJ 08544 USA

[3] Cornell High Energy Synchrotron Source, Ithaca, NY 14853 USA

来源：

JOURNAL OF CRYSTAL GROWTH | 2001年 / 232卷 / 1-4期

关键词：

crystal structure; growth from solution; biological macromolecules; lysozyme; proteins;

D O I：

10.1016/S0022-0248(01)01092-2

中图分类号：

O7 [晶体学];

学科分类号：

0702 ; 070205 ; 0703 ; 080501 ;

摘要：

We report preliminary measurements of the elastic properties of tetragonal lysozyme crystals using Brillouin scattering. This microscopic, non-contact technique is ideally suited for study of fragile, optically transparent macromolecular crystals. Brillouin scattering should allow much more complete characterization of crystal elasticity, and provide a novel probe of intermolecular interactions, conformation changes, and defect formation. (C) 2001 Elsevier Science B.V. All rights reserved.

引用

页码：498 / 501

页数：4

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