Extended Data Figure 1: PfRH5 disorder predictions and structural alignment.

a, Long-range disorder was predicted by POODLE-L¹⁹ and was used to determine domain boundaries for the PfRH5ΔNL crystallization construct. The disorder predictions are shown above the sequence of PfRH5, with values of >0.5 indicative of disorder. The residues visible in the PfRH5ΔNL crystal structure are shown below the PfRH5 sequence as secondary structure elements (sheets as blue arrows, and helices as tubes in rainbow colouring) linked by blue lines. The missing loop (248–296) is shown as a break in the blue line. The secretion signal sequence is indicated (black underline). b, Two copies of PfRH5 from the PfRH5–basigin structure (red and orange), two copies from the PfRH5–QA1 structure (blue and cyan), and one copy from PfRH5–9AD4 (green) structure were aligned using Coot³¹, giving an r.m.s.d. of 1.7 Å. The C terminus and the loop between helices 4 and 5 were the only regions showing significant differences. For the remaining 95% of PfRH5, the r.m.s.d. is 0.9 Å.