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
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
收藏
页码:498 / 501
页数:4
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