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Cloning, Expression, Purification, Crystallization and Preliminary Crystallographic Analysis of γ-­Filamin Repeat 23 by Ljiljana Sjekloća; Björn Sjöblom; Maurizio Polentarutti; Kristina Djinović Carugo is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is Cloning, Expression, Purification, Crystallization and Preliminary Crystallographic Analysis of γ-­Filamin Repeat 23 about?

Human -®lamin is a protein of 2705 amino-acid residues that localizes mainly in the myo®brillar Z-disc and to smaller extent in the subsarcolemmal region of striated muscle cells. -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. -Filamin repeat 23 was indicated as being necessary for binding to the muscle-speci®c subsarcolemmal proteins -and -sarcoglycan and the myo®brillar protein FATZ1. The recombinant -®lamin 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 A Ê resolution using 1.2 A Ê wavelength synchrotron radiation. Preliminary structural analysis shows one molecule, with predominantly secondary-structure elements, per asymmetric unit.

Who reads Cloning, Expression, Purification, Crystallization and Preliminary Crystallographic Analysis of γ-­Filamin Repeat 23?

Author

Ljiljana Sjekloća; Björn Sjöblom; Maurizio Polentarutti; Kristina Djinović Carugo

Publisher

International Union of Crystallography; Blackwell Publishing Inc.; International Union of Crystallography (IUCr) (ISSN 0907-4449)

Published

2004

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)