Induction of crystal nucleation by orientation-controlled binding of His6-tagged proteins to functionalized gold nanoparticles,CrystEngComm

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Induction of crystal nucleation by orientation-controlled binding of His6-tagged proteins to functionalized gold nanoparticles
CrystEngComm ( IF 2.6 ) Pub Date : 2020/01/08 , DOI: 10.1039/c9ce01786k
Jiyeon Park _{1,

2,

3,

4} , Tae Ho Kang _{1,

2,

3,

4} , Inhee Choi _{1,

2,

3,

4} , Jungwoo Choe _{1,

2,

3,

4}

Affiliation

Protein crystallization is an indispensable process in structural determination by crystallography and consists of nucleation and crystal growth. Nucleation, wherein protein monomers in solution cluster in an ordered fashion to form a stable nucleus, is a critical yet difficult step in crystallization. Herein, we utilized sphere-, star-, and rod-shaped gold nanoparticles (GNPs) functionalized with nitrilotriacetic acid (NTA) or citrate as nucleation cores and showed that the GNPs could facilitate nucleation by interacting with His₆-tagged proteins. Evaluation of the crystallization of two proteins indicated that GNPs significantly increased the number of crystallization conditions compared to that of the control. Furthermore, NTA-modified GNPs had better effect on crystallization than did citrate-capped GNPs, which could be attributed to orientation-controlled protein clustering around the GNPs by specific conjugation of NTA-modified GNP–Ni²⁺–His₆-tagged proteins. Our findings indicate that functionalized GNPs can greatly increase the success rate of protein crystallization and accelerate the structural determination process by X-ray crystallography.

中文翻译：

通过His6标签的蛋白质与功能化的金纳米粒子的方向控制结合来诱导晶体成核

蛋白质结晶是通过晶体学确定结构中必不可少的过程，由成核作用和晶体生长组成。成核是溶液中的关键但困难的步骤，其中溶液中的蛋白质单体以有序的方式聚集以形成稳定的核。在本文中，我们利用以次氮基三乙酸（NTA）或柠檬酸盐官能化的球形，星形和棒状金纳米颗粒（GNP）作为成核核心，并表明这些GNP可通过与His ₆相互作用来促进成核标记的蛋白质。对两种蛋白质结晶的评估表明，与对照相比，GNP显着增加了结晶条件的数量。此外，NTA修饰的GNP比柠檬酸盐封端的GNP具有更好的结晶效果，这可以归因于NTA修饰的GNP-Ni ²⁺ -His ₆标记蛋白的特异性结合，从而控制了GNP周围的蛋白质取向。我们的发现表明功能化的GNP可以大大提高蛋白质结晶的成功率，并通过X射线晶体学加快结构确定过程。

更新日期：2020-02-13

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