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Figure 4
Results obtained after applying the Zernike3D algorithm to a set of cryo-EM maps from the ryanodine receptor 1 (RyR1). The data set was constructed in such a way that there are always two maps corresponding to the same conformational state: an experimental cryo-EM map and a cryo-EM map simulated from the atomic structure associated with the previous experimental map. (a) A structure map obtained when comparing experimental cryo-EM maps (red dots) and atomic models (blue dots) for RyR1 through the deformation distance d1. The results show that the method succeeded in recovering most of the pairs defined by the experimental cryo-EM maps and atomic structures. (b) A structure map obtained when comparing experimental cryo-EM maps (red dots) and atomic models (blue dots) through the correlation distance. In this case, the correlation metric fails to recover the pairs but it identifies correctly the two different map types used for this analysis. (c) A consensus structure map resulting from the combination of (a) and (b). The consensus provides an optimal solution that helps to identify the map pairs and the map types by keeping a similar structural relationship in the blue and red branches. In these cases, none of these approaches are sufficient for creating a meaningful structure map based on conformation alone, leading us to apply the improvement in Fig. 5[link].

IUCrJ
Volume 8| Part 6| November 2021| Pages 992-1005
ISSN: 2052-2525
https://doi.org/10.1107/S2052252521008903