Fig. 1: Cryo-EM characterization of the PML RBCC domain. | Cell Discovery

Fig. 1: Cryo-EM characterization of the PML RBCC domain.

From: Cryo-EM structure of PML RBCC dimer reveals CC-mediated octopus-like nuclear body assembly mechanism

Fig. 1

a Depiction of full-length PML’s domain arrangement, highlighting the PML RBCC fragment (residues 46–256 used for structure determination). Different domains were depicted in distinct colors. b Cryo-EM density map of PML46–256 dimer. c Model-map fitting of the PML46–256 dimer. d XL-MS analysis of the MBP-PML46–256 monomer (left), with identified intra-subunit XLs also mapped on the PML46–256 monomer model and shown as black dotted lines (right). e XL-MS analysis of the MBP-PML46–256 dimer (left). Identified inter-subunit XLs were also mapped on the PML46–256 dimer model. Red and black dashed lines indicate XLs with Cα–Cα distances less than 35 Å and greater than 35 Å, respectively (right). We used the best E-value (1.00 × 10–2) and spec count of at least 2 as the threshold to remove XL-MS data with lower confidence. f Atomic model of the PML46–256 dimer, with each monomer colored in blue and green, and the secondary structure elements numbered as α1–α7 and β1–β7. The N-terminal P46 was marked as a yellow sphere, the C-terminal S221 as a red sphere, and the SUMO sites K65 and K160 as pink spheres.

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