Meyer Peter A, Ye Ping, Zhang Mincheng, Suh Man-Hee, Fu Jianhua
Department of Molecular Biology and Genetics, Cornell University, 221 Biotechnology Building, Ithaca, New York 14853, USA.
Structure. 2006 Jun;14(6):973-82. doi: 10.1016/j.str.2006.04.003.
Macromolecular assemblies as large as RNA polymerase II (Pol II) can be phased by a few intrinsically bound Zn atoms, by using MAD experiments as described here. A phasing effectiveness of 570 aa/Zn is attained for Pol II. The resulting experimental, unbiased electron density map is of such quality that it confirms the existing crystallographic model and further reveals structural regions not shown by model phases, thus updating the Pol II model at three sites. The mechanistically important fork loop-1 element is observed to be ordered in the absence of nucleic acids, suggesting additional insights into the mechanisms that maintain the stability of the transcription ternary complex and allow its release. Furthermore, a computational experiment with simulated MAD data sets demonstrates that 1 Zn site is able to provide adequate experimental phase information for as many as 1100 amino acids of polypeptide, under the conditions of the current synchrotron and detector technologies.
像RNA聚合酶II(Pol II)这样的大分子组装体可以通过此处所述的多波长反常散射(MAD)实验,利用几个内在结合的锌原子来进行相位确定。对于Pol II,实现了每锌原子570个氨基酸的相位确定效率。由此产生的实验性、无偏差的电子密度图质量很高,它证实了现有的晶体学模型,并进一步揭示了模型相位未显示的结构区域,从而在三个位点更新了Pol II模型。在没有核酸的情况下,观察到具有重要机制意义的叉状环-1元件是有序的,这为维持转录三元复合物稳定性并使其释放的机制提供了更多见解。此外,一项使用模拟MAD数据集的计算实验表明,在当前同步加速器和探测器技术条件下,1个锌位点能够为多达1100个氨基酸的多肽提供足够的实验相位信息。