ArticleActa crystallographica. Section F, Structural biology and crystallization communications2007
Expression, purification, crystallization and preliminary X-ray diffraction analysis of chloride intracellular channel 2 (CLIC2).
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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2 citing papers in PubMed, 7 citations in OpenAlex.
- Chloride intracellular channel 1 functions in endothelial cell growth and migration.Journal of angiogenesis research · 2010Article
- A rational free energy-based approach to understanding and targeting disease-causing missense mutations.Journal of the American Medical Informatics Association : JAMIAArticle
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7 authors at 2 institutions in 1 country.
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Abstract
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 A resolution. Crystal form A displayed P2(1)2(1)2(1) symmetry, with unit-cell parameters a = 44.0, b = 74.7, c = 79.8 A. Crystal form B displayed P2(1) symmetry, with unit-cell parameters a = 36.0, b = 66.9, c = 44.1 A. Structure determination will shed more light on the structure and function of this enigmatic family of proteins.
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