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The α subunit C-terminal domain (αCTD) of RNA polymerase (RNAP) is a key element in transcription activation inEscherichia coli, possessing determinants responsible for the interaction of RNAP with DNA and with transcription factors. Here, the crystal structure ofE. coliαCTD (α subunit residues 245–329) determined to 2.0 Å resolution is reported. Crystals were obtained after reductive methylation of the recombinantly expressed domain. The crystals belonged to space groupP21and possessed bothdoi:10.1107/s0907444910018470 pmid:20606261 pmcid:PMC2897699 fatcat:t2doshpmejelfnzfzyhog2ggve