Cantu-Bustos J Enrique, Cano Del Villar Kevin D, Vargas-Cortez Teresa, Morones-Ramirez Jose Ruben, Balderas-Renteria Isaias, Zarate Xristo
Universidad Autonoma de Nuevo Leon, Facultad de Ciencias Quimicas, Av. Universidad s/n, Ciudad Universitaria, San Nicolas de los Garza, Nuevo Leon 66451, Mexico.
Data Brief. 2016 Mar 4;7:502-8. doi: 10.1016/j.dib.2016.02.074. eCollection 2016 Jun.
Fusion proteins have become essential for the expression and purification of recombinant proteins in Escherichia coli. The metal-binding protein CusF has shown several features that make it an attractive fusion protein and affinity tag: "Expression and purification of recombinant proteins in Escherichia coli tagged with the metal-binding protein CusF" (Cantu-Bustos et al., 2016 [1]). Here we present accompanying data from protein expression experiments; we tested different protein tags, temperatures, expression times, cellular compartments, and concentrations of inducer in order to obtain soluble protein and low formation of inclusion bodies. Additionally, we present data from the purification of the green fluorescent protein (GFP) tagged with CusF, using Ag(I) metal affinity chromatography.
融合蛋白已成为在大肠杆菌中表达和纯化重组蛋白的关键。金属结合蛋白CusF展现出了几个特性，使其成为一种有吸引力的融合蛋白和亲和标签：“用金属结合蛋白CusF标记在大肠杆菌中表达和纯化重组蛋白”（坎图 - 布斯托斯等人，2016年[1]）。在此，我们展示了蛋白质表达实验的相关数据；我们测试了不同的蛋白质标签、温度、表达时间、细胞区室以及诱导剂浓度，以获得可溶性蛋白并减少包涵体的形成。此外，我们还展示了使用Ag(I)金属亲和层析法纯化用CusF标记的绿色荧光蛋白（GFP）的数据。
