Self-interaction chromatography: a novel screening method for rational protein crystallization.
Self-interaction chromatography: a novel screening method for rational protein crystallization.
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自相互作用色谱：一种合理蛋白质结晶的新型筛选方法。
DOI：
10.1107/s0907444902012775
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发表时间：
2002
期刊：
影响因子：
--
通讯作者：
Lenhoff,AbrahamM
中科院分区：
文献类型：
--
作者：
Tessier,PeterM;Vandrey,ScottD;Berger,BryanW;Pazhianur,Rajesh;Sandler,StanleyI;Lenhoff,AbrahamM
渗透第二维里系数，B22，已成为最广泛使用的数量在发展一个合理的理解蛋白质结晶。在这项工作中，提出了一种新的方法测量B22使用自相互作用色谱法（SIC），这是至少一个数量级比传统的表征方法，如静态光散射更有效。结果表明，SIC测量BSA的第二维里系数与静态光散射结果定量一致。BSA和肌红蛋白的测得维里系数揭示了硫酸铵的浓度范围令人惊讶地窄，这促进了对结晶最佳的弱吸引力相互作用。利用维里系数信息，合理、快速地进行了肌红蛋白超离心结晶。
The osmotic second virial coefficient, B22, has become the quantity most widely used in developing a rational understanding of protein crystallization. In this work a novel method of measuring B22 using self-interaction chromatography (SIC) is presented that is at least an order of magnitude more efficient than traditional characterization methods, such as static light scattering. It is shown that SIC measurements of second virial coefficients for BSA are in quantitative agreement with static light scattering results. The measured virial coefficient for both BSA and myoglobin reveal a surprisingly narrow range of concentrations of ammonium sulfate that promote weakly attractive interactions that are optimal for crystallization. Using the virial coefficient information, myoglobin crystals were obtained by ultracentrifugal crystallization in a rational and rapid manner.