Department of Crystallography, Birkbeck College, Malet St., London WC1E 7HX, UK.
Biochem Cell Biol. 2010 Feb;88(1):89-96. doi: 10.1139/o09-164.
Independent cryo electron microscopy (cryo-EM) studies of the closely related protein disaggregases ClpB and Hsp104 have resulted in two different models of subunit arrangement in the active hexamer. We compare the EM maps and resulting atomic structure fits, discuss their differences, and relate them to published experimental information in an attempt to discriminate between models. In addition, we present some general assessment criteria for low-resolution cryo-EM maps to offer non-structural biologists tools to evaluate these structures.
独立的冷冻电子显微镜（cryo-EM）研究表明，紧密相关的蛋白解聚酶 ClpB 和 Hsp104 在活性六聚体中具有两种不同的亚基排列模型。我们比较了 EM 图谱和由此产生的原子结构拟合，讨论了它们的差异，并将其与已发表的实验信息相关联，试图区分模型。此外，我们还提出了一些低分辨率 cryo-EM 图谱的一般评估标准，为非结构生物学家提供评估这些结构的工具。
