TABLE 2.
Crystallographic data collection and refinement statistics
| MASP-2·SGMI-2 complexa | MASP-1·SGMI-1 complexa | |
|---|---|---|
| Data collection | ||
| Space group | P212121 | P212121 |
| Cell dimensions a, b, c (Å) | 50.92, 62.47, 114.19 | 71.33, 98.40, 155.53 |
| Resolution (Å) | 39.55-1.28 (1.30-1.28) | 46.91-3.20 (3.37-3.20) |
| Rmeasb | 0.065 (0.752) | 0.258 (0.997) |
| I/σ I | 15.10 (2.54) | 7.6 (2.3) |
| Completeness (%) | 95.8 (93.3) | 99.9 (100.0) |
| Redundancy | 5.44 (5.06) | 6.8 (7.1) |
| Refinement | ||
| Resolution (Å) | 38.00-1.28 | 46.91-3.20 |
| No. reflections | 85,991 | 18,639 |
| Rwork/Rfreec | 0.156/0.205 | 0.228/0.274 |
| No. atoms | ||
| Protein | 2911 | 6463 |
| Ligand/ion | 5 | |
| Water | 534 | 2 |
| B-Factors (Å2) | ||
| Protein | 17.14 | 47.19 |
| Ligand/ion | 18.03 | |
| Water | 36.83 | 11.65 |
| Root mean square deviation | ||
| Bond lengths (Å) | 0.025 | 0.006 |
| Bond angles (°) | 2.059 | 1.036 |
| Ramachandran plotd | 269/27/2 | 629/95/1 |
| Molprobity score | 1.56 | 2.62 |
a One crystal was used for data collection. Values in parentheses are for highest resolution shell.
b Rmeas = Σhl[nh/(nh − 1)]1/2|Ihl − 〈Ih〉|/Σhl〈Ih〉, where nh is the number of observations of reflection h.
c R = Σh|Fo − Fc|/ΣhFo, Rwork= Rfactor for reflection included in refinement calculations, Rfree = R factor for a selected subset (5%) of the reflections that was not included in refinement calculations.
d Number of residues in most favored/allowed/disallowed regions.