Li Daoyi, Pérez María Muñoz, Zhang Xiaoqi, Li Jiaqing, Jiang Wen
Department of Biological Sciences, Purdue University, West Lafayette, IN 47907.
Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA 16802.
bioRxiv. 2025 May 23:2025.05.18.654508. doi: 10.1101/2025.05.18.654508.
Helical symmetry is a structural feature of many biological assemblies, including cytoskeletons, viruses, and pathological amyloid fibrils. One unique metadata for helical structures is the helical parameters, twist and rise. With the increasing number of helical structures being resolved through cryo-EM and deposited in the EMDB, there is a growing possibility of errors in the metadata associated with these entries. During our cryo-EM analysis of protein amyloids and the development of helical analysis tools, we realized that many deposited helical parameters appear inconsistent with the associated density maps. Herein, we have developed a comprehensive validation process that examines the consistency of these parameters by combining high-throughput computational evaluation with manual verification. Multiple errors were identified and corrected for ~14% of the total entries, including missing parameters, swapped twist and rise values, incorrect sign of twist angles, partial symmetries, and bona fide errors. Our validation code, workflow, and the validated parameters are publicly available.
螺旋对称是许多生物组装体的一种结构特征,包括细胞骨架、病毒和病理性淀粉样纤维。螺旋结构的一个独特元数据是螺旋参数,即扭转和上升。随着通过冷冻电镜解析并存储在EMDB中的螺旋结构数量不断增加,与这些条目不相关的元数据出现错误的可能性也在增加。在我们对蛋白质淀粉样纤维进行冷冻电镜分析以及开发螺旋分析工具的过程中,我们意识到许多存储的螺旋参数似乎与相关的密度图不一致。在此,我们开发了一个全面的验证过程,通过将高通量计算评估与人工验证相结合来检查这些参数的一致性。我们识别并纠正了约14%的总条目中的多个错误,包括缺失参数、扭转和上升值互换、扭转角符号错误、部分对称性以及真正的错误。我们的验证代码、工作流程以及经过验证的参数都是公开可用的。