title: Crystallization and preliminary X-ray diffraction studies of the tetramerization domain derived from the human potassium channel Kv1.3.
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.
authors: Department of Biophysics and Physical Biochemistry, University of Regensburg, D-93040 Regensburg, Germany.
authors: Andreas
authors: A
authors: Winklmeier
authors: Michael
authors: M
authors: Weyand
authors: Christina
authors: C
authors: Schreier
authors: Hans Robert
authors: HR
authors: Kalbitzer
authors: Werner
authors: W
authors: Kremer
mesh_terms: D003460:Crystallization; D006801:Humans; D051664:Kv1.3 Potassium Channel / Q000737:chemistry*; D055503:Protein Multimerization; D017434:Protein Structure, Tertiary; D014961:X-Ray Diffraction
chemical_list: D051664:Kv1.3 Potassium Channel