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. 2020 Oct 13;3:568. doi: 10.1038/s42003-020-01283-8

Table 2.

X-ray data collection and refinement statistics.

PfELC-N Complex 1 Complex 1f Complex 2 P. falciparum complexa
Data collection
Space group P 21 21 21 P 41 P 41 I 21 21 21 P 43
Cell dimensions
 a, b, c (Å) 30.24, 57.51, 86.34 87.32, 87.32, 56.75 86.13, 86.13, 53.7 84.63, 93.48, 108.15 211.88 211.88 75.46
 α, β, γ (°) 90, 90, 90 90, 90, 90 90, 90, 90 90, 90, 90 90, 90, 90
Resolution (Å) 47.86–1.50  (1.55–1.50) 47.58–2.39 (2.48–2.39) 40.94–2.00 (2.07–2.00) 40.96–2.30 (2.38–2.30) 47.42–2.51 (2.58–2.51)
Rmerge 0.03382 (0.495) 0.106 (1.599) 0.0431 (1.35) 0.08044 (1.007) 0.0874 (3.79)
I / σI 17.68 (2.06) 19.06 (1.40) 31.02 (1.74) 13.84 (1.79) 12.69 (0.55)
Completeness (%) 99.0 (98.0) 99.9 (99.7) 99.9 (99.4) 99.9 (99.9) 83.5 (8.0)
Total no. reflections 104329 (9981) 226789 (23610) 373831 (34891) 124597 (12474) 768342 (75189)
Redundancy 4.2 (4.2) 13.3 (13.7) 13.5 (12.9) 6.4 (6.6) 6.7 (6.6)
Refinement
Resolution (Å) 1.5 2.4 2.0 2.3 2.5
No. reflections 104329 226789 373831 124597 768342
Rwork / Rfree 0.167/0.193 0.189/0.231 0.190/0.225 0.186/0.219 0.200/0.238
No. atoms 1319 2523 2610 2687 12968
 Protein 1126 2457 2458 2578 12965
 Ligands n.a. 2 5 33 n.a.
 Solvent 193 64 147 76 3
B-factors 36.5 78.2 65.4 65.3 99.69
 Proteins 34.8 78.3 65.4 65.0 99.69
 Ligands n.a. 96.6 111 94.2 n.a.
 Solvent 46.5 72.8 63.2 62.6 70.51
R.m.s. deviations
 Bond lengths (Å) 0.013 0.008 0.003 0.007 0.015
 Angles (°) 1.16 0.97 0.60 0.87 2.04

aThe native data of the P. falciparum complex  were subjected to anisotropic scaling and truncation. Without truncation, II of the native data set used for refinement falls below 2.0 between a maximum resolution of 2.75 and 2.70 Å at an overall completeness of over 99%.