ArticleActa crystallographica. Section F, Structural biology and crystallization communications2005
Overexpression, purification, crystallization and preliminary X-ray diffraction analysis of the C-terminal domain of Ss-LrpB, a transcription regulator from Sulfolobus solfataricus.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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1 citing paper in PubMed.
- Nanobody(R)-based chromatin immunoprecipitation/micro-array analysis for genome-wide identification of transcription factor DNA binding sites.Nucleic acids research · 2013Article
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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 alphabeta-sandwich (betaalphabetabetaalphabeta 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 P2(1)2(1)2, with unit-cell parameters a = 59.35, b = 74.86, c = 38.08 A and a data set was collected to 2.0 A resolution. Structure determination using a selenomethionine derivative is under way.
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