Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8359687 | Protein Expression and Purification | 2016 | 20 Pages |
Abstract
KcsA, the bacterial K+ channel from Streptomyces lividans, is the prototypical model system to study the functional and structural correlations of the pore domain of eukaryotic voltage-gated K+ channels (Kv channels). It contains all the molecular elements responsible for ion conduction, activation, deactivation and inactivation gating [1]. KcsA's structural simplicity makes it highly amenable for structural studies. Therefore, it is methodological advantageous to produce large amounts of functional and properly folded KcsA in a cost-effective manner. In the present study, we show an optimized protocol for the over-expression and purification of large amounts of high-quality, fully functional and crystallizable KcsA using inexpensive detergents, which significantly lowered the cost of the purification process.
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Authors
Cholpon Tilegenova, Spandana Vemulapally, Doris M. Cortes, Luis G. Cuello,