Open AccessCrystallization and preliminary X‐ray diffraction studies of the tetramerization domain derived from the human potassium channel Kv1.3
Author(s) -
Winklmeier Andreas,
Weyand Michael,
Schreier Christina,
Kalbitzer Hans Robert,
Kremer Werner
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109019514
Subject(s) - potassium , crystallography , crystallization , potassium channel , domain (mathematical analysis) , chemistry , resolution (logic) , synchrotron radiation , potassium phosphate , diffraction , biophysics , biology , physics , optics , chromatography , mathematical analysis , mathematics , organic chemistry , artificial intelligence , computer science
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 m M potassium phosphate pH 6.5 in the absence of additional precipitants. The crystals showed I 4 symmetry characteristic of the naturally occurring tetrameric assembly of the single subunits. A complete native data set was collected to 1.2 Å resolution at 100 K using synchrotron radiation.