Open AccessCrystallization and preliminary X‐ray crystallographic analysis of ligand‐free and arginine‐bound forms of Thermotoga maritima arginine‐binding protein
Author(s) -
Ruggiero Alessia,
Dattelbaum Jonathan D.,
Pennacchio Anna,
Iozzino Luisa,
Staiano Maria,
Luchansky Matthew S.,
Der Bryan S.,
Berisio Rita,
D'Auria Sabato,
Vitagliano Luigi
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309111037341
Subject(s) - thermotoga maritima , arginine , crystallization , crystallography , chemistry , ligand (biochemistry) , biochemistry , stereochemistry , amino acid , escherichia coli , organic chemistry , receptor , gene
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.