Article: article from journal or magazin.
Crystallization and preliminary crystallographic characterization of an SH3 domain from the IB1 scaffold protein.
Acta crystallographica. Section D, Biological crystallography
Publication types: Journal Article ; Research Support, Non-U.S. Gov't - Publication Status: ppublish
IB1 is a mammalian scaffold protein that interacts with components of the c-Jun N-terminal kinase (JNK) signal-transduction pathway mainly via its protein-protein interaction domains. Crystallization of the key Src homology 3 (SH3) domain of IB1 has been achieved. Crystallization experiments with unmodified protein and deliberately oxidized protein have led to different crystal forms. X-ray data have been collected to 3.0 A resolution from a crystal form with rectangular prism morphology. These crystals are orthorhombic (P2(1)2(1)2(1)), with unit-cell parameters a = 45.9, b = 57.0, c = 145.5 A. These are the first crystallographic data on a scaffold molecule such as IB1 to be reported.
Crystallization, Crystallography, X-Ray, Nuclear Proteins, Recombinant Fusion Proteins, Selenomethionine, Trans-Activators, src Homology Domains
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