Protein crystallization: from purified protein to diffraction-quality crystal
Protein crystallization: from purified protein to diffraction-quality crystal
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DOI：
10.1038/nmeth.f.203
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发表时间：
2008-02-01
期刊：
影响因子：
48
通讯作者：
Saridakis, Emmanuel
中科院分区：
文献类型：
--
作者：
Chayen, Naomi E.;Saridakis, Emmanuel
X射线晶体学测定生物大分子的结构涉及一系列步骤：目标分子的选择;克隆、表达、纯化和结晶;衍射数据的收集和原子位置的确定。然而，即使有纯的可溶性蛋白质，生产高质量的晶体仍然是结构测定的主要瓶颈。在这里，我们提出了一个指导非专家筛选适当的结晶条件和优化衍射质量的晶体生长。
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.