Crystallization and preliminary X-ray diffraction analysis of the arginine repressor of the hyperthermophile Thermotoga neapolitana

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
Jan MassantDominique Maes

Abstract

The arginine repressor of Thermotoga neapolitana (ArgRTnp) is a member of the family of multifunctional bacterial arginine repressors involved in the regulation of arginine metabolism. This hyperthermophilic repressor shows unique DNA-binding features that distinguish it from its homologues. ArgRTnp exists as a homotrimeric protein that assembles into hexamers at higher protein concentrations and/or in the presence of arginine. ArgRTnp was crystallized with and without its corepressor arginine using the hanging-drop vapour-diffusion method. Crystals of the aporepressor diffracted to a resolution of 2.1 A and belong to the orthorhombic P2(1)2(1)2(1) space group, with unit-cell parameters a = 117.73, b = 134.15, c = 139.31 A. Crystals of the repressor in the presence of its corepressor arginine diffracted to a resolution of 2.4 A and belong to the same space group, with similar unit-cell parameters.

References

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Feb 22, 2002·Acta Crystallographica. Section D, Biological Crystallography·Caitríona A Dennis CSimon E V Phillips
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Mar 8, 2005·The Journal of Biological Chemistry·Rasmus LarsenOscar P Kuipers
Apr 5, 2005·Acta Crystallographica. Section D, Biological Crystallography·Airlie J McCoyRandy J Read

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