Table 1.
Data collection and refinement statistics
| PatGmac | PatGmac + peptide | |
|---|---|---|
| Data collectiona,b | ||
| Space group | C2 | C2 |
| Cell dimensions | ||
| a, b, c (Å) | 132.08, 67.58, 97.34 | 135.63, 67.32, 137.87 |
| α, β, γ (°) | 90.0, 115.01, 90.0 | 90.0, 116.76, 90.0 |
| Resolution (Å) | 2.19 (2.24–2.19) | 2.63 (2.77–2.63) |
| Rmerge | 6.1 (49.8) | 10.7 (52.2) |
| I / σI | 13.7 (2.9) | 10.1 (2.3) |
| Completeness (%) | 99.5 (98.8) | 99.3 (96.4) |
| Redundancy | 3.6 (3.5) | 3.7 (3.1) |
| Refinement | ||
| Resolution (Å) | 33.79–2.19 | 21.42–2.63 |
| No. reflections | 38,196 | 31,502 |
| Rwork / Rfree | 0.203 / 0.224 | 0.191 / 0.218 |
| No. atoms | 4,877 | 5,108 |
| Protein | 4,653 | 4,897 |
| Ligand/ion | – | 69 |
| Water | 224 | 142 |
| B factors | 50.11 | 60.56 |
| Protein | 50.04 | 60.70 |
| Ligand/ion | – | 77.98 |
| Water | 51.5 | 47.19 |
| R.m.s. deviations | ||
| Bond lengths (Å) | 0.009 | 0.009 |
| Bond angles (°) | 1.249 | 1.253 |
a
One crystal user per structure.
b
Values in parentheses are for highest-resolution shell.