Open AccessOverexpression, purification, crystallization and preliminary X‐ray diffraction analysis of the C‐terminal domain of Ss‐LrpB, a transcription regulator from Sulfolobus solfataricus
Author(s) -
Peeters Eveline,
Hoa Bach Thi Mai,
Zegers Ingrid,
Charlier Daniel,
Maes Dominique
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309105032148
Subject(s) - sulfolobus solfataricus , sulfolobus , transcription (linguistics) , escherichia coli , crystallization , dna binding domain , chemistry , archaea , crystallography , transcription factor , biology , microbiology and biotechnology , biochemistry , gene , organic chemistry , linguistics , philosophy
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 αβ‐sandwich (βαββαβ 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 P 2 1 2 1 2, 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.