Table 1. Data collection and refinement statistics.
| PEPC crystal | C3 (F. pringlei) | C3truncated | C4 (F. trinervia) |
|---|---|---|---|
| Data collection | |||
| Space group | P21212 | P21212 | P21212 |
| Cell dimensions | |||
| a, b, c (Å) | 164.8, 121.6, 132.9 | 165.6, 121.7, 132.0 | 162.5, 122.1, 131.9 |
| α,β,γ (°) | 90.0, 90.0, 90.0 | 90.0, 90.0, 90.0 | 90.0, 90.0, 90.0 |
| Resolution (Å)* | 48.93−3.20 (3.37−3.20) | 165.55−2.71 (2.86−2.71) | 37.83−2.49 (2.62−2.49) |
| Rmeas | 0.130 (0.438) | 0.102 (0.344) | 0.099 (0.397) |
| I/σI† | 6.0 (1.9) | 6.3 (2.0) | 5.9 (2.0) |
| Completeness (%) | 99.9 (100) | 100 (100) | 100 (100) |
| Redundancy | 3.7 (3.8) | 15.8 (16.4) | 26.2 (24.0) |
| Refinement | |||
| Resolution (Å)* | 70.1−2.71 (2.78−2.71) | 37.0−2.49 (2.55−2.49) | |
| No. of reflections | 71548 (1486) | 90203 (1845) | |
| Rwork/Rfree | 0.188 (0.226)/0.230 (0.275) | 0.204 (0.241)/0.237 (0.292) | |
| No. of atoms | |||
| Protein | 14750 | 14710 | |
| Ligand/ion | 46 | 36 | |
| Water | 56 | 198 | |
| B-factors‡ | |||
| Protein | 75.0 | 60.4 | |
| Ligand/ion | 51.8 | 39.1 | |
| Water | 34.3 | 37.3 | |
| R.m.s.d. | |||
| Bond lengths (Å) | 0.016 | 0.017 | |
| Bond angles (°) | 1.758 | 1.794 | |
r.m.s.d., root-mean-square deviation.
A single crystal was used for each data set.
*Highest resolution shell is shown in parenthesis.
†Signal-to-noise ratio of merged intensities.
‡Protein B factors are calculated as the sum of the contribution from the TLS parameters and the residual B factors.