Acta Crystallographica Section F

Structural Biology and Crystallization Communications

Volume 61, Part 11 (November 2005)

crystallization communications

 

Overexpression, purification, crystallization and preliminary X-ray diffraction analysis of the C-terminal domain of Ss-LrpB, a transcription regulator from Sulfolobus solfataricus

E. Peeters, B. T. M. Hoa, I. Zegers, D. Charlier and D. Maes

Abstract: Ss-LrpB from Sulfolobus solfataricus P2 belongs to the bacterial/archaeal superfamily of Lrp-like (leucine-responsive regulatory protein-like) transcription regulators. The N-terminal DNA-binding domain contains a HTH motif and the C-terminal domain contains an -sandwich ( fold). The C-terminal domain was overexpressed in Escherichia coli, purified and crystallized using the hanging-drop vapour-diffusion method. The crystals belong to space group P2₁2₁2, with unit-cell parameters a = 59.35, b = 74.86, c = 38.08 Å and a data set was collected to 2.0 Å resolution. Structure determination using a selenomethionine derivative is under way.

Keywords: Ss-LrpB; transcription regulators.

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