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. 2018 Oct 15;37(22):e100005. doi: 10.15252/embj.2018100005

Figure 3. SPIN90 binds to the front side of Arp2/3 complex.

Figure 3

  1. Ribbon diagram of Arp2/3 complex with bound SPIN90 from the co‐complex structure. SPIN90 is shown in pink with cylindrical helices. Conventional designations of “Front”, “Back”, and “Bottom” views are indicated in right panel.
  2. Ribbon diagram showing front side of Arp2/3 complex and bound SPIN90 with Fo−Fc electron density map contoured at 2.1 σ calculated without phases from SPIN90 (chain M).
  3. Model of bovine Arp2/3 complex with bound WASP CA segments modeled based on crosslinking/mass‐spectrometry, homology modeling, x‐ray crystallography, and FRET (Padrick et al, 2011; Ti et al, 2011; Boczkowska et al, 2014; Jurgenson & Pollard, 2015; Rodnick‐Smith et al, 2016a; Luan et al, 2018). The complex is in an identical orientation to the right panel in (A).
  4. Surface representation of model described in (C) showing the convention for front, back, and bottom views of Arp2/3 complex.