The arginine-binding protein from Thermotoga maritima (TmArgBP) is an arginine-binding component of the ATP-binding cassette (ABC) transport system in this hyperthermophilic bacterium. This protein is endowed with an extraordinary stability towards thermal and chemical denaturation. Its structural characterization may provide useful insights for the clarification of structure– stability relationships and for the design of new biosensors. Crystallization trials were set up for both arginine-bound and ligand-free forms of TmArgBP and crystals suitable for crystallographic investigations were obtained for both forms. Ordered crystals of the arginine adduct of TmArgBP could only be obtained by using the detergent LDAO as an additive to the crystallization medium. These crystals were hexagonal, with unit-cell parameters a = 78.2, c = 434.7 Å, and diffracted to 2.7 Å resolution. The crystals of the ligand-free form were orthorhombic, with unit-cell parameters a = 51.8, b = 91.9, c = 117.9 Å , and diffracted to 2.25 Å resolution.
Copyright © 2011 International Union of Crystallography. This article first appeared in Acta Crystallographica Section F Structural Biology and Crystallization Communications F67 (2011), 1462-1465.
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Ruggiero, Alessia, Jonathan D. Dattelbaum, Anna Pennacchio, Luis Iozzino, Maria Staiano, Matthew S. Luchansky, Bryan S. Der, Rita Berisio, Sabato D'Auria, and Luigi Vitagliano. "Crystallization and Preliminary X-ray Crystallographic Analysis of Ligand-free and Arginine-bound Forms of Thermotoga Maritima Arginine-binding Protein." Acta Crystallographica Section F Structural Biology and Crystallization Communications F67 (2011): 1462-465. doi:10.1107/S1744309111037341.