Abstract
Regulator of K+ conductance (RCK) domains form a conserved class of ligand-binding domains that control the activity of a variety of prokaryotic and eukaryotic K+ channels. Structural analysis of these domains by X-ray crystallography has provided insight toward mechanisms underlying ligand binding and channel gating, and thus the experimental strategies aimed at determining structures of liganded and unliganded forms of the domains may be useful in analysis of other ligand-binding domains. Here, we describe a basic strategy for crystallographic analysis of the RCK domain from the MthK channel, for determination of its Ca2+-bound structure.
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Acknowledgements
We wish to thank Karin Abarca-Heidemann, Andrew S. Thomson, Matthew M. Callaghan, and Elsie Samakai for technical expertise and helpful discussions. This work was supported by NIH grant R01 GM68523 to B.S.R.
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Smith, F.J., Rothberg, B.S. (2013). Analysis of Ca2+-Binding Sites in the MthK RCK Domain by X-Ray Crystallography. In: Gamper, N. (eds) Ion Channels. Methods in Molecular Biology, vol 998. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-62703-351-0_22
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DOI: https://doi.org/10.1007/978-1-62703-351-0_22
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