Purification, crystallization and preliminary X-ray diffraction of wild-type and mutant recombinant human transforming growth factor beta-induced protein (TGFBIp)

Transforming growth factor β-induced protein (TGFBIp) has been linked to several corneal dystrophies as certain point mutations in the protein may give rise to a progressive accumulation of insoluble protein material in the human cornea. Little is known about the biological functions of this extracellular protein, which is expressed in various tissues throughout the human body. However, it has been found to interact with a number of extracellular matrix macromolecules such as collagens and proteoglycans. Structural information about TGFBIp might prove to be a valuable tool in the elucidation of its function and its role in corneal dystrophies caused by mutations in the TGFBI gene. A simple method for the purification of wild-type and mutant forms of recombinant human TGFBIp from human cells under native conditions is presented here. Moreover, the crystallization and preliminary X-ray analysis of TGFBIp are reported. © 2009 International Union of Crystallography All rights reserved.
This work was supported by National Eye Institute Grant R01 EY 12712, the Danish National Research Foundation, the Danish Natural Science Research Council, the Danish Association for Prevention of Eye Diseases and Blindness, the Synoptik Foundation, Aarhus University Research Foundation and the Danish Medical Research Council. Further support was provided by BIO2006-02668, PSE-010000-2007-1 and the CONSOLIDER-INGENIO 2010 Project 'La Factoría de Cristalización' (CSD2006-00015) from Spanish public agencies, FP6 Strep Project LSHG-2006-018830 'CAMP' and FPT Collaborative Project 223101 'AntiPathoGN' from the European Union and 2005SGR00280 from the National Catalan Government