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. 2021 Jun 8;40(14):e106438. doi: 10.15252/embj.2020106438

Figure EV2. Related to Fig 2. Comparison of Bax (α2–α5) dimer structures in bicelles (yellow) to crystal structures of Bax (α2–α5) (cyan) and Bak (α2–α5) (salmon) dimers.

Figure EV2

  • A
    Three‐dimensional structure superposition of the structure of Bax (α2–α5) in bicelles determined by NMR (yellow; PDB code: 6L8V) and the structure determined by crystallography in the absence of membranes (cyan; PDB code: 4BDU).The RMSD value between the superimposed protein backbones is 3.878 Å. Note that the residues from K123 to S126 form an extra α helical turn (orange) in the NMR structure.
  • B
    Three‐dimensional structure superposition of the bicelle‐bound structure of Bax (α2–α5) (yellow; PDB code: 6L8V) and the Bak (α2–α5) dimer structure determined by crystallography in the absence of membranes (salmon; PDB code: 4U2V). The RMSD value between the superimposed protein backbones is 5.177 Å.