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  • Title: Purification, crystallization and initial crystallographic analysis of RNA polymerase holoenzyme from Thermus thermophilus.
    Author: Vassylyeva MN, Lee J, Sekine SI, Laptenko O, Kuramitsu S, Shibata T, Inoue Y, Borukhov S, Vassylyev DG, Yokoyama S.
    Journal: Acta Crystallogr D Biol Crystallogr; 2002 Sep; 58(Pt 9):1497-500. PubMed ID: 12198314.
    Abstract:
    RNA polymerase holoenzyme from Thermus thermophilus, consisting of six protein subunits (alpha(2), beta, beta', omega and sigma(70)) and having a total molecular mass of about 450 kDa, was purified and crystallized by the hanging-drop vapour-diffusion technique under mild near-physiological conditions. The crystals diffract beyond 3 A resolution. Careful analysis of diffraction data revealed that the crystals belong to space group P3(2), with unit-cell parameters a = b = 236.35, c = 249.04 A, and have perfect twinning along the threefold axis. A complete data set at 3 A resolution was collected and an unambiguous molecular-replacement solution was found using the structure of T. aquaticus RNA polymerase core enzyme as a search model. The refinement of structure and model building of the sigma(70) subunit is now in progress.
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