Cloning, expression, purification, crystallization and preliminary crystallographic analysis of gamma-filamin repeat 23.

Human gamma-filamin is a protein of 2705 amino-acid residues that localizes mainly in the myofibrillar Z-disc and to smaller extent in the subsarcolemmal region of striated muscle cells. gamma-Filamin consists of an N-terminal actin-binding domain followed by a long rod-shaped region. The rod-shaped region consists of 24 immunoglobulin-like domains that form a platform for interaction with different transmembrane, cell-signalling and cytoskeletal proteins. gamma-Filamin repeat 23 was indicated as being necessary for binding to the muscle-specific subsarcolemmal proteins gamma- and delta-sarcoglycan and the myofibrillar protein FATZ1. The recombinant gamma-filamin repeat 23 was crystallized using the hanging-drop vapour-diffusion method, which yielded needle-shaped diffraction-quality crystals. Diffraction data were collected to 2.05 angstroms resolution using 1.2 angstroms wavelength synchrotron radiation. Preliminary structural analysis shows one molecule, with predominantly beta secondary-structure elements, per asymmetric unit. Copyright 2004 International Union of Crystallography