Journal
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
Volume 58, Issue -, Pages 1497-1500Publisher
BLACKWELL MUNKSGAARD
DOI: 10.1107/S0907444902011770
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Funding
- NIGMS NIH HHS [GM54098-06A1] Funding Source: Medline
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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 Angstrom 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 Angstrom, and have perfect twinning along the threefold axis. A complete data set at 3 Angstrom 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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