Table 3.
Data collection and refinement statistics (molecular replacement)
| H6-PduA K26A (crystal form 1) |
H6-PduA K26A (crystal form 2) |
|
|---|---|---|
| Data collection | ||
| Space group | C2 | F23 |
| Cell dimensions | ||
| a, b, c (Å) | 183.2, 105.4, 67.3 | 235.3, 235.3, 235.3 |
| α, β ,γ (°) | 90.0, 94.8, 90.0 | 90.0, 90.0, 90.0 |
| Resolution (Å) | 1.94 (2.01–1.94)* | 2.4 (2.486–2.4) |
| Rmerge | 0.077 (0.523) | 0.076 (0.981) |
| Rpim | 0.059(0.373) | 0.017 (0.234) |
| I / σI | 15.6 (2.2) | 33.9 (4.2) |
| Completeness (%) | 96.4 (97.2) | 100.0 (100.0) |
| Redundancy | 4.1 (4.0) | 20.5 (20.6) |
| Wilson B-factor | 32.5 Å2 | 52.3 Å2 |
| Refinement | ||
| Resolution (Å) | 1.94 | 2.4 |
| No. reflections | 89773 | 42124 |
| Rwork / Rfree | 0.194/0.209 | 0.195/0.219 |
| No. atoms | ||
| Protein | 5662 | 4305 |
| Ligand/ion | 81 | 47 |
| Water | 260 | 62 |
| B-factors | ||
| Protein | 47.5 | 62.5 |
| Ligand/ion | 63.6 | 83.8 |
| Water | 47.4 | 48.7 |
| R.m.s. deviations | ||
| Bond lengths (Å) | 0.010 | 0.002 |
| Bond angles (°) | 1.2 | 0.58 |
One crystal for each structure was used for data collection and structure determination.
*
Highest-resolution shell is shown in parentheses.