@article{493172ca39824e5f922a9e4894c0ecbb,
title = "Crystallization and preliminary crystallographic characterization of an SH3 domain from the IB1 scaffold protein",
abstract = "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.",
keywords = "Crystallization, Crystallography, X-Ray, Nuclear Proteins, Recombinant Fusion Proteins, Selenomethionine, Trans-Activators, src Homology Domains",
author = "Imran Dar and Christophe Bonny and Pedersen, {Jan Torleif} and Michael Gajhede and Ole Kristensen",
year = "2003",
doi = "10.1107/S0907444903020304",
language = "English",
volume = "59",
pages = "2300--2",
journal = "Acta Crystallographica Section D: Structural Biology",
issn = "2059-7983",
publisher = "International Union of Crystallography",
number = "Pt 12",
}