Table 1. Data collection and refinement statistics.
| DENV2 sE A259C–EDE2 A11 Fab fragment (PDB 5N0A) | DENV2 sE L107C/A313C–EDE2 A11 Fab fragment (PDB 5N09) | |
|---|---|---|
| Data collection | ||
| Space group | P 21 21 2 | P 21 21 2 |
| Cell dimensions | ||
| a, b, c (Å) | 182.3, 208.7, 58.8 | 180.6, 205, 58.9 |
| α, β, γ (°) | 90, 90, 90 | 90, 90, 90 |
| Resolution (Å) | 50−3.9 (4.1−3.9)* | 50−3.9 (4.3−3.9)* |
| Anisotropy directions | ||
| Resolution where CC1/2>0.30 | ||
| overall (Å) | 3.9 | 3.9 |
| along h axis (Å) | 3.9 | 3.9 |
| along k axis (Å) | 7.2 | 6.2 |
| along l axis (Å) | 3.9 | 3.9 |
| Rmerge | 0.31 (0.84) | 0.69 (1.97) |
| Rmeas | 0.41 (1.08) | 0.84 (2.42) |
| Rpim | 0.26 (0.68) | 0.48 (1.4) |
| <I/σ(I) > | 3.1 (1.4) | 2.4 (0.7) |
| Mn(I) half-set correlation | 0.95 (0.68) | 0.89 (0.51) |
| Completeness (%) | 96.9 (97.5) | 96.9 (98.0) |
| Redundancy | 3.8 (3.8) | 5.1 (4.9) |
| Refinement | ||
| Resolution | 20.0−3.9 (4.1−3.9)† | 40.0−3.9 (4.1−3.9) |
| No. of reflections (Work/Test) | 19,112/947 | 19,323/945 |
| Rwork / Rfree | 0.29/0.30 (0.27/0.31) | 0.31/0.35 (0.37/0.38) |
| No. of atoms (protein) | ||
| Protein | 9542 | 12683 |
| Glycans | 143 | 157 |
| Water | 0 | 2 |
| R.m.s deviations | ||
| Bond lengths (Å) | 0.007 | 0.005 |
| Bond angles (deg) | 1.13 | 1.20 |
CC1/2, correlation coefficient; PDB, Protein Data Bank; Rmeas, multiplicity-corrected R; Rpim, expected precision.
The high-resolution limit used for refinement after anisotropy statistics is shown in bold.
*Highest resolution shell is shown in parenthesis.
†Low-resolution for refinement of DENV2 sE A259C–EDE2 A11 Fab complex was truncated to 20 Å.