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Updated: Jun 21, 2026
Reconstitution of a Kv Channel into Lipid Membranes for Structural and Functional Studies
Published on: July 13, 2013
Crystallization and preliminary X-ray diffraction studies of the tetramerization domain derived from the human
Andreas Winklmeier1, Michael Weyand, Christina Schreier
1Department of Biophysics and Physical Biochemistry, University of Regensburg, D-93040 Regensburg, Germany.
Abstract:
The tetramerization domain (T1 domain) derived from the voltage-dependent potassium channel Kv1.3 of Homo sapiens was recombinantly expressed in Escherichia coli and purified. The crystals were first grown in an NMR tube in 150 mM potassium phosphate pH 6.5 in the absence of additional precipitants. The crystals showed I4 symmetry characteristic of the naturally occurring tetrameric assembly of the single subunits. A complete native data set was collected to 1.2 A resolution at 100 K using synchrotron radiation.
