Remis Jonathan, Petrov Petar N, Zhang Jessie T, Axelrod Jeremy J, Cheng Hang, Sandhaus Shahar, Mueller Holger, Glaeser Robert M
Department of Physics, University of California Berkeley, Berkeley, CA 94720, USA.
Lawrence Berkeley National Laboratory, One Cyclotron Road, Berkeley, CA 94720, USA.
bioRxiv. 2024 Aug 6:2024.08.04.606536. doi: 10.1101/2024.08.04.606536.
Apoferritin (apoF) is commonly used as a test specimen in single-particle electron cryo-microscopy (cryo-EM), since it consistently produces density maps that go to 3 Å resolution or higher. When we imaged apoF with a laser phase plate (LPP), however, we observed more severe particle-to-particle variation in the images than we had previously thought to exist. Similarly, we found that images of ribulose bisphosphate carboxylase/oxygenase (rubisco) also exhibited a much greater amount of heterogeneity than expected. By comparison to simulations of images, we verified that the heterogeneity is not explained by the known features of the LPP, shot noise, or differences in particle orientation. We also demonstrate that our specimens are comparable to those previously used in the literature, based on using the final-reconstruction resolution as the metric for evaluation. All of this leads us to the hypothesis that the heterogeneity is due to damage that has occurred either during purification of the specimen or during preparation of the grids. It is not, however, our goal to explain the causes of heterogeneity; rather, we report that using the LPP has made the apparent damage too obvious to be ignored. In hindsight, similar heterogeneity can be seen in images of apoF and the 20S proteasome which others had recorded with a Volta phase plate. We therefore conclude that the increased contrast of phase-plate images (at low spatial frequencies) should also make it possible to visualize, on a single-particle basis, various forms of biologically functional heterogeneity in structure that had previously gone unnoticed.
脱铁铁蛋白(apoF)常用于单颗粒电子冷冻显微镜(cryo-EM)测试样本,因为它始终能生成分辨率达到3埃或更高的密度图。然而,当我们用激光相位板(LPP)对apoF成像时,我们观察到图像中颗粒间的差异比我们之前认为存在的更为严重。同样,我们发现核酮糖二磷酸羧化酶/加氧酶(rubisco)的图像也表现出比预期大得多的异质性。通过与图像模拟比较,我们证实这种异质性不能用LPP的已知特征、散粒噪声或颗粒取向差异来解释。基于将最终重建分辨率作为评估指标,我们还证明我们的样本与文献中先前使用的样本相当。所有这些使我们提出一个假设,即这种异质性是由于样本纯化过程中或网格制备过程中发生的损伤所致。然而,解释异质性的原因并非我们的目标;相反,我们报告使用LPP使明显的损伤变得太明显而无法忽视。事后看来,在其他人用伏打相位板记录的apoF和20S蛋白酶体的图像中也能看到类似的异质性。因此,我们得出结论,相位板图像(在低空间频率下)对比度的增加也应该能够在单颗粒基础上可视化以前未被注意到的各种生物功能结构异质性形式。