Protein crystallization: from purified protein to diffraction-quality crystal

被引：270

作者：

Chayen, Naomi E. ^{[1
]}

Saridakis, Emmanuel ^{[2
]}

机构：

[1] Univ London Imperial Coll Sci Technol & Med, Fac Med, Dept Biomol Med, Div Surg Oncol Reprod Biol & Anaesthet, London SW7 2AZ, England

[2] Natl Ctr Sci Res Demokritos, Inst Phys Chem, Lab Struct & Supramol Chem, Athens 15310, Greece

来源：

NATURE METHODS | 2008年 / 5卷 / 02期

基金：

英国工程与自然科学研究理事会;

关键词：

D O I：

10.1038/NMETH.F.203

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Determining the structure of biological macromolecules by X-ray crystallography involves a series of steps: selection of the target molecule; cloning, expression, purification and crystallization; collection of diffraction data and determination of atomic positions. However, even when pure soluble protein is available, producing high-quality crystals remains a major bottleneck in structure determination. Here we present a guide for the non-expert to screen for appropriate crystallization conditions and optimize diffraction-quality crystal growth.

引用

页码：147 / 153

页数：7

共 62 条

[1] PROTEIN CRYSTAL-GROWTH - AN APPROACH BASED ON PHASE-DIAGRAM DETERMINATION [J].