ArticleProtein expression and purification2016
An improved method for the cost-effective expression and purification of large quantities of KcsA.
Article in Protein expression and purification, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Expression and Purification of the Human Voltage-Gated Proton Channel (hHBio-protocol · 2025Article
- A novel method for expressing and purifying large quantities of functional and stable human voltage-gated proton channel (hHProtein science : a publication of the Protein Society · 2025Article
- Characterization of a novel MgtE homolog and its structural dynamics in membrane mimetics.Biophysical journal · 2024Article
- The nonconducting W434F mutant adopts upon membrane depolarization an inactivated-like state that differs from wild-type Shaker-IR potassium channels.Science advances · 2022Article
- Cost-effective Purification of Membrane Proteins using a Dual-detergent Strategy.Current protocols · 2022Article
- Biochemical and biophysical characterization of a prokaryotic MgProtein expression and purification · 2019Article
- Structure, function, and ion-binding properties of a KProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Inverted allosteric coupling between activation and inactivation gates in KProceedings of the National Academy of Sciences of the United States of America · 2018Article
- A cost-effective protocol for the over-expression and purification of fully-functional and more stable Erwinia chrysanthemi ligand-gated ion channel.Protein expression and purification · 2017Article
- Activation of the mechanosensitive ion channel MscL by mechanical stimulation of supported Droplet-Hydrogel bilayers.Scientific reports · 2017Article
- Hysteresis of KcsA potassium channel's activation- deactivation gating is caused by structural changes at the channel's selectivity filter.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
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Authors and funding
4 authors.
Funding
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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