Protein crystallization: from purified protein to diffraction-quality crystal

被引：241
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
收藏
页码：147 / 153
页数：7
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