Yuyama Ken-Ichi, Chang Kai-Di, Tu Jing-Ru, Masuhara Hiroshi, Sugiyama Teruki
Department of Applied Chemistry, National Chiao Tung University, 1001 Ta Hsueh Rd, Hsinchu, 30010, Taiwan.
Phys Chem Chem Phys. 2018 Feb 28;20(9):6034-6039. doi: 10.1039/c7cp06990a.
Confining protein crystallization to a millimetre size was achieved within 0.5 h after stopping 1 h intense trapping laser irradiation, which shows excellent performance in spatial and temporal controllability compared to spontaneous nucleation. A continuous-wave near-infrared laser beam is tightly focused into a glass/solution interfacial layer of a supersaturated buffer solution of hen egg-white lysozyme (HEWL). The crystallization is not observed during laser trapping, but initiated by stopping the laser irradiation. The generated crystals are localized densely in a circular area with a diameter of a few millimetres around the focal spot and show specific directions of the optical axes of the HEWL crystals. To interpret this unique crystallization, we propose a mechanism that nucleation and the subsequent growth take place in a highly concentrated domain consisting of HEWL liquid-like clusters after turning off laser trapping.
在停止1小时的强捕获激光照射后0.5小时内，实现了将蛋白质结晶限制在毫米尺寸内，与自发成核相比，这在空间和时间可控性方面表现出优异的性能。连续波近红外激光束被紧密聚焦到蛋清溶菌酶（HEWL）过饱和缓冲溶液的玻璃/溶液界面层中。在激光捕获过程中未观察到结晶现象，但在停止激光照射后开始结晶。生成的晶体密集地定位在焦点周围直径为几毫米的圆形区域内，并显示出HEWL晶体光轴的特定方向。为了解释这种独特的结晶现象，我们提出了一种机制，即在关闭激光捕获后，成核和随后的生长发生在由HEWL类液体簇组成的高浓度区域中。
