Crystallization and preliminary X-ray crystallographic analysis of ligand-free and arginine-bound forms of Thermotoga maritima arginine-binding protein (Articolo in rivista)

Type
Label
  • 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)
Pagina inizio
  • 1462 (literal)
Pagina fine
  • 1465 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 1 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali
  • 4 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 67 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • 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)
Prodotto di
Autore CNR

Incoming links:


Autore CNR di
Prodotto
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi
data.CNR.it