Crystallization and preliminary X‐ray diffraction analysis of the DNA‐binding domain of the response regulator SaeR from Staphylococcus epidermidis

Publisher: John Wiley & Sons Inc

E-ISSN: 1744-3091|69|6|689-691

ISSN: 1744-3091

Source: Acta Crystallographica Section F, Vol.69, Iss.6, 2013-06, pp. : 689-691

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Abstract

SaeR is the response regulator of the SaeRS two‐component signal transduction system, which is involved in regulating bacterial autolysis and biofilm formation. SaeR comprises an N‐terminal receiver domain and a C‐terminal effector domain. The effector domain possesses DNA‐binding and transactivation functions. Here, the effector domain of SaeR from Staphylococcus epidermidis was purified and crystallized using the sitting‐drop vapour‐diffusion method. The crystals diffracted to a resolution of 2.15 Å and belonged to space group P212121, with unit‐cell parameters a = 34.20, b = 53.78, c = 111.66 Å. Determining the structure will provide insights into the mechanisms underlying DNA binding.

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