Supplementary Figure 23 Helium ion microscopy (HIM) buffer and non-phosphorylated controls preclude salt precipitation

<b> Helium ion microscopy (HIM) buffer and non-phosphorylated controls preclude salt precipitation. </b>In order to determine that our proteins were forming fractal-like patterns and it was not salt inducing the patterns, a buffer and non-phosphorylated proteins sample controls were used to preclude salt precipitation. (<b>A</b>) Usual HIM square salt crystals on a glass surface. (<b>B</b>) Deposited HNG buffer (50 mM Hepes, 100 mM NaCl, 5% glycerol, pH.7.4, buffer proteins are stored in) on silicon wafer shows no structures on the surface. (<b>C</b>) 3 µM non-pY-AtzAM1 and 2 µM AtzCM1 control shows no fractal-like structures. (<b>D</b>) 3 µM non-pY-AtzAM1 and 1 µM AtzCM1 show no fractal-like structures. All controls demonstrate that fractal structures are formed by phosphorylated protein components.

<b>氦离子显微镜（Helium ion microscopy, HIM）缓冲液与非磷酸化对照可排除盐析干扰。</b>为验证本研究中蛋白质所形成的类分形结构并非由盐类诱导产生，实验采用缓冲液与非磷酸化蛋白质样品作为对照以排除盐析干扰。(<b>A</b>) 玻璃表面的典型方形盐晶体（氦离子显微镜成像）。(<b>B</b>) 硅片上沉积的HNG缓冲液（本实验蛋白质储存所用缓冲液：50 mM 羟乙基哌嗪乙磺酸（Hepes）、100 mM 氯化钠、5%甘油，pH 7.4）表面未观测到任何结构。(<b>C</b>) 浓度为3 μM的非磷酸化AtzAM1（non-pY-AtzAM1）与2 μM的AtzCM1对照样品，未呈现类分形结构。(<b>D</b>) 浓度为3 μM的非磷酸化AtzAM1与1 μM的AtzCM1样品，未观测到类分形结构。所有对照实验均证实，类分形结构由磷酸化蛋白质组分所形成。