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Probing the quality of crystals of biological macromolecules using maximum resolution of diffraction data, Bragg reflection profiles and X-ray topographs

被引：20
作者：
Fourme, R
Ducruix, A
Riès-Kautt, M
Capelle, B
机构：
[1] Univ Paris Sud, MENRT, CEA, CNRS,LURE, F-91405 Orsay, France
[2] CNRS, Lab Enzymol & Biochim Struct, F-91198 Gif Sur Yvette, France
[3] Univ Paris 06, CNRS, Lab Mineral & Cristallog, F-75252 Paris, France
[4] Univ Denis Diderot, F-75252 Paris 05, France
来源：
JOURNAL OF CRYSTAL GROWTH | 1999年 / 196卷 / 2-4期
关键词：
crystal growth; crystal perfection; protein crystal; topograph; lysozyme; collagenase;
D O I：
10.1016/S0022-0248(98)00876-8
中图分类号：
O7 [晶体学];
学科分类号：
0702 ; 070205 ; 0703 ; 080501 ;
摘要：
The quality of a macromolecular crystal can be probed by combining maximum resolution of diffraction data, Bragg reflection profiles and X-ray topographs. Concerning maximum resolution, critical parameters are the overall rms displacement of atoms, which includes both dynamic and static disorder components, and the dynamic range of integrated intensities that can be achieved for given sample and experimental conditions. Bragg reflection profiles and topographs recorded with a quasi-plane wave of X-rays give a wealth of information on the domain structure and macroscopic disorder. (C) 1999 Published by Elsevier Science B.V. All rights reserved.
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收藏
页码：535 / 545
页数：11
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