http://www.cnr.it/ontology/cnr/individuo/prodotto/ID214437
Crystallization and preliminary X-ray crystallographic analysis of ligand-free and arginine-bound forms of Thermotoga maritima arginine-binding protein (Articolo in rivista)
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- Crystallization and preliminary X-ray crystallographic analysis of ligand-free and arginine-bound forms of Thermotoga maritima arginine-binding protein (Articolo in rivista) (literal)
- Anno
- 2011-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1107/S1744309111037341 (literal)
- Alternative label
Ruggiero A, Dattelbaum JD, Pennacchio A, Iozzino L, Staiano M, Luchansky MS,nDer BS, Berisio R, D'Auria S, Vitagliano L (2011)
Crystallization and preliminary X-ray crystallographic analysis of ligand-free and arginine-bound forms of Thermotoga maritima arginine-binding protein
in Acta crystallographica. Section F
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Ruggiero A, Dattelbaum JD, Pennacchio A, Iozzino L, Staiano M, Luchansky MS,nDer BS, Berisio R, D'Auria S, Vitagliano L (literal)
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- Institute of Biostructures and Bioimaging, CNR, Via Mezzocannone 16, I-80134 Naples, Italy. (literal)
- Titolo
- Crystallization and preliminary X-ray crystallographic analysis of ligand-free and arginine-bound forms of Thermotoga maritima arginine-binding protein (literal)
- Abstract
- 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. (literal)
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