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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机译：RNA聚合酶全酶从栖热菌属酸奶,6个蛋白亚基组成(α(2),β,β,ω和σ(70))有一个总约450 kDa的分子质量,纯化和结晶的悬滴vapour-diffusion技术在温和的near-physiological条件。衍射超出3一项决议。晶体的衍射数据显示属于空间群P3(2),与单胞参数a = b = 236.35, c = 249.04,完美的双晶沿着三轴。收集完整的数据集在3一项决议和一个明确的molecular-replacement解决方案被发现使用t . aquaticus RNA的结构吗聚合酶的核心酶作为搜索模型。优化的结构和模型建立σ(70)亚基现在在进步。
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