Effective protein crystallization using crystal hysteresis

被引：9

作者：

Adachi, H

Takano, K

Yoshimura, M

Mori, Y

Sasaki, T

机构：

[1] Osaka Univ, Grad Sch Engn, Dept Elect Engn, Suita, Osaka 5650871, Japan

[2] Osaka Univ, Venture Business Lab, Suita, Osaka 5650871, Japan

[3] Osaka Univ, Grad Sch Engn, Dept Mat & Life Sci, Suita, Osaka 5650871, Japan

[4] JST, PRESTO, Suita, Osaka 5650871, Japan

来源：

JAPANESE JOURNAL OF APPLIED PHYSICS PART 2-LETTERS | 2003年 / 42卷 / 4A期

关键词：

protein crystal growth; slow cooling; lysozyme; cooling rate; hysteresis;

D O I：

10.1143/JJAP.42.L384

中图分类号：

O59 [应用物理学];

学科分类号：

摘要：

We have developed a new method for protein crystallization, crystal hysteresis, that utilizes slow-cooling and recooling techniques. Slow cooling of a saturated solution enables precise control of supersaturation in the solution and also allows reuse of the solution because it maintains its composition. Examination of the effects of various cooling rates on hen egg-white lysozyme crystallization revealed that the cooling rate determined the number and size of the obtained crystals. Furthermore, recrystallization of lysozyme from the same solution after dissolving the previously grown crystals was to found to be very effective in reducing the number of nucleation sites, thus obtaining larger crystals.

引用

页码：L384 / L385

页数：2

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