ArticleActa crystallographica. Section F, Structural biology and crystallization communications2011
Crystallization and preliminary X-ray crystallographic analysis of ligand-free and arginine-bound forms of Thermotoga maritima arginine-binding protein.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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5 citing papers in PubMed.
- The non-swapped monomeric structure of the arginine-binding protein from Thermotoga maritima.Acta crystallographica. Section F, Structural biology communications · 2019Article
- The characterization of Thermotoga maritima Arginine Binding Protein variants demonstrates that minimal local strains have an important impact on protein stability.Scientific reports · 2019Article
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- Periplasmic Binding Proteins in Thermophiles: Characterization and Potential Application of an Arginine-Binding Protein from Thermotoga maritima: A Brief Thermo-Story.Life (Basel, Switzerland) · 2013Review
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10 authors.
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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.
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