Extended Data Fig. 1: Comparison of apo PolθH tetramer cryo-EM and crystal structures. | Nature Structural & Molecular Biology

Extended Data Fig. 1: Comparison of apo PolθH tetramer cryo-EM and crystal structures.

From: Human polymerase θ helicase positions DNA microhomologies for double-strand break repair

Extended Data Fig. 1

a, Coomassie-stained SDS-PAGE of proteins used in this study. This experiment was independently repeated three times with similar results. WT: PolθH amino acids 2–894. ΔLH: PolθH with amino acids 838–860 deleted. ΔD5: PolθH amino acids 2–789. 2 µg of protein was loaded in each well. b, In the PolθH tetramer cryo-EM structure, two dimeric PolθH subunits are rotated about 4º with respect to the crystal structure (PDB: 5A9J). Residues 35–66 are omitted from the crystal structure representation.

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