Extended Data Fig. 2: Cryo-EM of Cor–RP2. | Nature

Extended Data Fig. 2: Cryo-EM of Cor–RP2.

From: Structures of an RNA polymerase promoter melting intermediate elucidate DNA unwinding

Extended Data Fig. 2

a, Angular distribution calculated in cryoSPARC for particle projections. Heat map shows number of particles for each viewing angle. b, Gold-standard FSC41, calculated by comparing the two independently determined half maps from cryoSPARC. The dotted line represents the 0.143 FSC cut-off which indicates a nominal resolution of 3.6 Å. c, FSC calculated between the refined structure and the half map used for refinement (work, red), the other half map (free, blue) and the full map (black). d, Top left, the 3.6 Å-resolution cryo-EM density map of Cor–RP2. Top right, a cross-section of the structure, showing the DNA inside the RNAP cleft. Bottom, same views as above, but coloured by local resolution35. The boxed region in the right view is magnified on the far right and sliced at the level of the Cor-binding pocket. Density for the Cor molecule is outlined in red. e, Left, overview of the Cor–RP2 structure, shown as a molecular surface. The boxed region is magnified on the right. Right, magnified view of the Cor-binding pocket in the same orientation as the boxed region on the left. Proteins are shown as α-carbon backbone worms. Residues that interact with Cor are shown in stick format. Cor is shown in stick format with green carbon atoms. Hydrogen bonds are indicated by dashed grey lines. The cryo-EM difference density for the Cor is shown as green mesh.