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High Protein-Loading Silica Template for Heterogeneous Protein Crystallization

机译：高蛋白质加载二氧化硅模板，用于异质蛋白质结晶

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摘要

As a purification technology, crystallization is advantageous over chromatography and precipitation in terms of purity, cost, and scalability. In general, proteins have slow crystallization kinetics due to their complex configurations, but this problem can be overcome with heterogeneous nucleants. High protein-loading mesoporous silica is a promising nucleant due to its favorable interaction with protein. The current study employs such a template in the batch crystallization of lysozyme and thaumatin at 1 mL scale. Using lysozyme as the main model protein, the results show that the template had high protein loading (220-300 mg lysozyme/g silica) and induced significantly faster crystallization as compared to the unseeded samples over a wide range of initial protein concentration (10.0-47.5 mg/mL) at 25 degrees C with 0.5 M potassium sodium tartrate tetrahydrate (precipitant) concentration. It was found that the template had to be saturated with the target protein before the experiments to achieve faster kinetics, or else it could delay the crystallization process. These findings were reaffirmed by the crystallization experiments of thaumatin. The current study demonstrates the effectiveness of high protein-loading silica as a nucleant in protein crystallization and the importance of its pretreatment with the target protein.
机译：作为纯化技术，结晶在纯度，成本和可扩展性方面的色谱和沉淀是有利的。通常，由于其复杂的构造，蛋白质具有缓慢的结晶动力学，但是这种问题可以通过异质核酸核肉克服。高蛋白质加载介孔二氧化硅是一种有前途的核素，由于其与蛋白质的良好相互作用。目前的研究采用溶菌酶的批量结晶和1mL标度的批量结晶的模板。使用溶菌酶作为主要模型蛋白质，结果表明，与未初始蛋白质浓度的未发现样品相比，模板具有高蛋白质载荷（220-300mg溶菌酶/ g二氧化硅），并诱导明显更快的结晶（10.0- 47.5mg / ml）在25℃下，具有0.5米的酒钾四水合物（沉淀剂）浓度。结果发现，在实验之前必须用靶蛋白饱和，以实现更快的动力学，否则它可能会延迟结晶过程。通过Thaumatin的结晶实验重新确定了这些发现。目前的研究证明了高蛋白质加载二氧化硅的有效性作为蛋白质结晶中的核素，其预处理与靶蛋白的预处理的重要性。

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