Kim Han-Ul, Jeong Myeong Seon, An Mi Young, Park Yoon Ho, Park Sun Hee, Chung Sang J, Yi Yoon-Sun, Jun Sangmi, Kim Young Kwan, Jung Hyun Suk
Department of Biochemistry, College of Natural Sciences, Kangwon National University, Chuncheon 24341, Republic of Korea.
Kangwon Center for Systems Imaging, Chuncheon 24341, Republic of Korea.
Int J Mol Sci. 2024 Dec 23;25(24):13731. doi: 10.3390/ijms252413731.
Recent advances in cryo-electron microscopy (cryo-EM) have facilitated the high-resolution structural determination of macromolecular complexes in their native states, providing valuable insights into their dynamic behaviors. However, insufficient understanding or experience with the cryo-EM image processing parameters can result in the loss of biological meaning. In this paper, we investigate the dihydrolipoyl acetyltransferase (E2) inner core complex of the pyruvate dehydrogenase complex (PDC) and reconstruct the 3D maps using five different symmetry parameters. The results demonstrate that the reconstructions yield structurally identical 3D models even at a near-atomic structure. This finding underscores a crucial message for researchers engaging in single-particle analysis (SPA) with relatively user-friendly and convenient image processing software. This approach helps reduce the risk of missing critical biological details, such as the dynamic properties of macromolecules.
冷冻电子显微镜（cryo-EM）的最新进展有助于在天然状态下对大分子复合物进行高分辨率结构测定，从而为其动态行为提供有价值的见解。然而，对冷冻电子显微镜图像处理参数的理解不足或经验欠缺可能导致生物学意义的丧失。在本文中，我们研究了丙酮酸脱氢酶复合物（PDC）的二氢硫辛酰乙酰转移酶（E2）内核复合物，并使用五种不同的对称参数重建了三维图谱。结果表明，即使在接近原子结构的情况下，重建也能产生结构相同的三维模型。这一发现为使用相对用户友好且便捷的图像处理软件进行单颗粒分析（SPA）的研究人员强调了一个关键信息。这种方法有助于降低遗漏关键生物学细节（如大分子的动态特性）的风险。
