Table 1 Data collection and refinement statistics
From: Structural insights into the non-inhibitory mechanism of the anti-EGFR EgB4 nanobody
| Â | EGFR-EgB4-EGF | EgB4 |
|---|---|---|
Data collection | ||
 Space group | P 61 2 2 | P 1 21 1 |
 Cell dimensions | ||
  a, b, c (Å) | 307.61, 307.61, 135.14 | 38.54, 71.58, 53.20 |
  α, β, γ (°) | 90.0, 90.0, 120.0 | 90.0, 91.5, 90.0 |
 Resolution (Å) | 153.81 - 6.05 (7.15 - 6.05) | 42.69 - 1.48 (1.50 - 1.48) |
 No. observed reflections | 60,948 (6230) | 162,212 (7549) |
 No. unique reflections | 6321 (632) | 47,214 (2189) |
 Rmerge | 0.187 (1.995) | 0.125 (1.681) |
 Mean I/σI | 7.8 (1.6) | 5.4 (1.1) |
 CC1/2 | 0.996 (0.548) | 0.990 (0.277) |
 Spherical completeness (%) | 65.3 (17.0) | 98.0 (93.0) |
 Ellipsoidal completeness (%) | 91.8 (63.9) | n/a |
 Ellipsoidal resolution limits (Å) [direction] | 7.25 [a*] | n/a |
7.25 [b*] | ||
6.02 [c*] | ||
 Redundancy | 9.6 (9.9) | 3.4 (3.4) |
Refinement | ||
 Resolution (Å) | 153.81 - 6.05 | 42.69 - 1.48 |
 Rwork/Rfree (%) | 29.6 / 32.7 | 17.7 / 20.5 |
 Average B-factors (Å2) | ||
  Protein | 534 | 17.4 |
  Glycans/ions/ligands | 591 | 15.7 |
  Water | n/a | 26.5 |
 R.M.S. deviations | ||
  Bond lengths (Å) | 0.0021 | 0.0122 |
  Bond angles (°) | 0.57 | 1.68 |
 Ramachandran (%) | ||
  Favored | 94.0 | 97.2 |
  Allowed | 5.9 | 2.8 |
  Outliers | 0.1 | 0 |
 Molprobity score | 1.59 | 1.21 |