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.

中文翻译：

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通过激光捕获快速溶菌酶的局部结晶†

在停止1 h强力捕获激光照射后的0.5 h内，将蛋白质结晶限制在毫米大小，与自发成核相比，它在空间和时间可控性方面表现出出色的性能。连续波近红外激光束紧紧聚焦在鸡蛋蛋白溶菌酶（HEWL）的过饱和缓冲溶液的玻璃/溶液界面层中。在激光捕获期间未观察到结晶，而是通过停止激光辐照而开始结晶。产生的晶体密集地定位在围绕焦点的直径为几毫米的圆形区域中，并显示HEWL晶体的光轴的特定方向。为了解释这种独特的结晶，