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Figure 5
Results obtained after applying the Zernike3D algorithm to a set of cryo-EM maps from the ryanodine receptor 1 (RyR1) followed by a decomposition of the distance matrix computed by the algorithm into different blocks to recover more meaningful structure mappings. (Top) A partition of the distance matrix into 2 × 2 blocks. Each block stores the distances obtained when comparing the different map types used in this test (pairs of experimental cryo-EM maps and maps derived from atomic structures representing the same conformational state): AA (atomic versus atomic), AC (atomic versus cryo-EM), CA (cryo-EM versus atomic) and CC (cryo-EM versus cryo-EM). (Bottom) A consensus structure map for pairs of RyR1 conformations (from atomic model-derived simulated maps and from cryo-EM maps) resulting from the analysis of the blocks. The red circles are used to enhance the visualization of the different pairs. When compared with Fig. 4[link](a), it is possible to see that this decomposition of the distance matrix leads to a proper recovering of all the pairs found in the data set.

Volume 8| Part 6| November 2021| Pages 992-1005
ISSN: 2052-2525