Open AccessExpression, purification, crystallization and preliminary X‐ray diffraction analysis of chloride intracellular channel 2 (CLIC2)
Author(s) -
Cromer Brett A.,
Gorman Michael A.,
Hansen Guido,
Adams Julian J.,
Coggan Marjorie,
Board Philip G.,
Parker Michael W.
Publication year - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309107049159
Subject(s) - crystallization , intracellular , diffraction , resolution (logic) , crystallography , crystal structure , chemistry , membrane , biophysics , materials science , biology , biochemistry , physics , optics , organic chemistry , artificial intelligence , computer science
The chloride intracellular channel (CLIC) family of proteins are unusual in that they can exist in either an integral membrane‐channel form or a soluble form. Here, the expression, purification, crystallization and preliminary diffraction analysis of CLIC2, one of the least‐studied members of this family, are reported. Human CLIC2 was crystallized in two different forms, both in the presence of reduced glutathione and both of which diffracted to better than 1.9 Å resolution. Crystal form A displayed P 2 1 2 1 2 1 symmetry, with unit‐cell parameters a = 44.0, b = 74.7, c = 79.8 Å. Crystal form B displayed P 2 1 symmetry, with unit‐cell parameters a = 36.0, b = 66.9, c = 44.1 Å. Structure determination will shed more light on the structure and function of this enigmatic family of proteins.