Extended Data Fig. 7: Cryo-EM raw data and summary of the 2:1 Chd1[L886G/L889G/L891G]-nucleosome complexes. | Nature Structural & Molecular Biology

Extended Data Fig. 7: Cryo-EM raw data and summary of the 2:1 Chd1[L886G/L889G/L891G]-nucleosome complexes.

From: A competitive regulatory mechanism of the Chd1 remodeler is integral to distorting nucleosomal DNA

Extended Data Fig. 7

a. Representative 2D class averages of (2:1) Chd1-nucleosome 2.61 Å structure generated from the final particles used for the reconstruction of the complex. b. Four orthogonal views of the (2:1) Chd1-nucleosome 2.61 Å structure. Coloring of Chd1 domains is given in 1D schematic. c. Representation of the Euler angle distribution of the final particles in the (2:1) Chd1-nucleosome 2.61 Å structure. The length of each cylinder representing a specific orientation is proportional to the number of particles. d. Local resolution of the (2:1) Chd1-nucleosome 2.61 Å structure, colored in accordance with the resolution values (Å), from highest (blue) to lowest (red). e. Fourier Shell Correlation (FSC) curve of the (2:1) Chd1-nucleosome 2.61 Å structure, calculated between two independent half maps from the refinement in CryoSPARC at the FSC cutoff 0.143. f. Conical FSC (cFSC) curve of the (2:1) Chd1-nucleosome 2.61 Å structure, calculated between two independent half maps with a conical mask of a specified half angle and axis in Fourier space, calculated in CryoSPARC. The cFSC shows correlations at each spacial frequency and the spread of resolution values over direction. The mean of the correlations at each spacial frequency are shown by the blue line, the minimum and maximum by the light blue shading, and the standard deviation by the dark blue shading. The crossings of 0.143 are given by the green histogram. g. Representative 2D class averages of (2:1) Chd1-nucleosome 2.88 Å structure, including a well-resolved DNA-binding domain, generated from the final particles used for the reconstruction of the complex. h. Four orthogonal views of the 2.88 Å structure. i. Representation of the Euler angle distribution of final particles in the (2:1) Chd1-nucleosome 2.88 Å complex with a well-resolved DNA-binding domain. The length of each cylinder representing a specific orientation is proportional to the number of particles. j. Local resolution of the (2:1) Chd1-nucleosome 2.88 Å complex with a well-resolved DNA-binding domain, colored in accordance with the resolution values (Å), from highest (blue) to lowest (red). k. Fourier Shell Correlation (FSC) curve of the (2:1) Chd1-nucleosome 2.88 Å complex with a well-resolved DNA-binding domain, calculated between two independent half maps from the refinement in CryoSPARC at the FSC cutoff 0.143. l. Conical FSC (cFSC) curve of the (2:1) Chd1 nucleosome 2.88 Å structure with a well-resolved DNA-binding domain, calculated between two independent half maps with a conical mask of a specified half angle and axis in Fourier space, calculated in CryoSPARC. The mean of the correlations at each spacial frequency are shown by the blue line, the minimum and maximum by the light blue shading, and the standard deviation by the dark blue shading. The crossings of 0.143 are given by the green histogram. Lines and arrows indicate the axis of rotation between subsequent views. Cryo-EM statistics are given in Table 1.

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