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. 2021 Feb 17;118(8):e2024512118. doi: 10.1073/pnas.2024512118

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Copyright © 2021 the Author(s). Published by PNAS.

This open access article is distributed under Creative Commons Attribution License 4.0 (CC BY).

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Fig. 6. — Cryo-EM structure of SHLD2L.3–REV7₂–TRIP13(E253Q) complex. (A) Schematic drawing of REV7, SHLD2L.3, and TRIP13 (E253Q) proteins involved in complex formation. Note that SHLDL2.3 contains a longer version (residues 1 to 50) of SHLD2 compared with SHLD2.3 (residues 1 to 19 of SHLD2). (B) Copurification of the complex formed by TRIP13(E253Q) hexamer and SHLD2L.3–REV7₂ in the presence of ATPγS by size exclusion chromatography. (C and D) The overall structure of the SHLD2L.3–REV7₂–TRIP13(E253Q) complex with bound ATPγS shown in electron density representations. Three different classes of structures of the complex with different twist and tilt between the SHLD2L.3–REV7₂ and TRIP13 (E253Q) components are shown with side (C) and top (D) views.