A new approach to the measurement of protein solubility by Michaelson interferometry
A new approach to the measurement of protein solubility by Michaelson interferometry
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DOI：
10.1016/s0022-0248(01)01142-3
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发表时间：
2001-11-01
影响因子：
1.8
通讯作者：
DeLucas, LJ
中科院分区：
文献类型：
--
作者：
Gray, RJ;Hou, WB;DeLucas, LJ
蛋白质浓度影响成核和晶体生长速率，因此适当的过饱和度对于制备大且优质的晶体至关重要。了解蛋白质溶解度对温度、pH 或离子强度等溶液变量的依赖性对于确定蛋白质晶体生长工作的最佳条件非常有用。我们改进了 Sazaki 等人报告的迈克尔逊干涉测量技术。 (J. Crystal Growth 169 (1996) 355.) 通过检查表面和浓度梯度条纹的行为，使用蛋白质溶菌酶和马血清白蛋白测定蛋白质溶解度。这使用小晶体 (0.2 mm x 0.1 mm) 提供了对蛋白质溶解度的灵敏且准确的估计。 (C) 2001 Elsevier Science B.V. 保留所有权利。
Protein concentration influences nucleation and crystal growth rates, therefore an appropriate degree of supersaturation is essential for the preparation of large and good quality crystals. Knowledge of a protein's solubility dependence on solution variables such as temperature, pH, or ionic strength can be very useful for defining optimum conditions for protein crystal growth work. We have refined a Michaelson interferometry technique reported by Sazaki et al. (J. Crystal Growth 169 (1996) 355.) for determination of protein solubility using the proteins lysozyme and equine serum albumin by examining the behavior of both surface and concentration gradient fringes. This has provided a sensitive and accurate estimate of protein solubility using small crystals (0.2 mm x 0.1 mm). (C) 2001 Elsevier Science B.V. All rights reserved.