Table 1.
Data collection and refinement statistics.
| Beamline | ID29 ESRF Grenoble, France |
|---|---|
| Space group | R3 |
| Unit-cell parameter (Å) | a = 203.83, c = 124.79, γ = 120° |
| Wavelength (Å) | 0.9737 |
| Resolution range (Å)* | 100–2.67 (2.70–2.67) |
| Redundancy | 12.6 |
| Completeness (%) | 98.4 (95.2) |
| Rmerge (%) | 6.0 (32.3) |
| Rmeas. (%)a | 14.1 (70.0) |
| (I)/(Is) | 15.45 (3.21) |
| Rcryst (%); (no. of reflections) | 27.50 (53,216) |
| Rfree (%); (no. of reflections)b | 30.60 (1547) |
| Twin fraction | 0.187, 0.257, 0.178, 0.377 |
| R.m.s.d bond length (target) (Å) | 0.004 (0.005) |
| R.m.s.d bond angle distances (target) (Å) | 0.012 (0.012) |
| No. of protein atoms | 8,289 |
| No. of solvent atoms | 79 |
| Ramachandran plot (%)c | |
| Most favoured regions | 78.3 |
| Allowed regions | 20.4 |
| Generously allowed regions | 1.3 |
| Disallowed regions | 0.0 |
a
The measured R-factor was calculated as described.54
b
The data set for the calculation of Rfree included for each randomly selected reflection its twin-related mate and all symmetry equivalents. The target r.m.s. deviation from ideal values corresponds to an effective weighting of that restrained in least-squares calculations. R.m.s. deviation for bond angles expressed in terms of 1–3 separation.
c
As defined by PROCHECK.52
*
Values in brackets belong to the highest resolution shell.