Protein crystallization by capillary counterdiffusion for applied crystallographic structure determination

被引:102
作者
Ng, JD [1 ]
Gavira, JA
García-Ruíz, JM
机构
[1] Univ Alabama, Dept Biol Sci, Huntsville, AL 35899 USA
[2] Univ Alabama, Struct Biol Lab, Huntsville, AL 35899 USA
[3] UGRA, CSIC, Fac Ciencias, Lab Estudios Cristalog,IACT, Granada 18002, Spain
基金
美国国家航空航天局;
关键词
protein crystallization; counterdiffusion; cryocrystallography; high throughput; crystallization cassette;
D O I
10.1016/S1047-8477(03)00052-2
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
Counterdiffusion crystallization in capillary is a very simple, cost-effective, and practical procedure for obtaining protein crystals suitable for X-ray data analysis. Its principles have been derived using well-known concepts coupling the ideas of precipitation and diffusion mass transport in a restricted geometry. The counterdiffusion process has been used to simultaneously screen for optimal conditions for protein crystal growth, incorporate strong anomalous scattering atoms, and mix in cryogenic solutions in a single capillary tube. The crystals obtained in the capillary have been used in situ for X-ray analysis. The implementation of this technique linked to the advancement of current crystallography software leads to a powerful structure determination method consolidating crystal growth, X-ray data collection, and ab initio phase determination into one without crystal manipulation. We review the historical progress of counterdiffusion crystallization, its application to X-ray crystallography, and ongoing too] development for high-throughput protein structure determination. (C) 2003 Elsevier Science (USA). All rights reserved.
引用
收藏
页码:218 / 231
页数:14
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