TABLE 2.
Data collection and refinement statistics
| Data set | Data |
|---|---|
| Space group | C2 |
| Cell parameters | a = 118.7 Å, b = 65.4 Å, c = 118.0 Å, β = 92.8° |
| Beamline at ESRFa | BM30A |
| Resolution (Å) | 30.0-2.0 |
| Completeness (%)b | 99.4 (99.4) |
| Total no. of observations | 193,166 |
| No. of unique reflections | 61,998 |
| Redundancyb | 3.1 (3.1) |
| Rsym (%)b,c | 5.7 (11.9) |
| I/σb | 7.5 (5.9) |
| Refinement | |
| Resolution (Å) | 15.0-2.0 |
| Total no. of protein atoms | 7,884 |
| No. of water molecules | 549 |
| R.m.s.d. from ideal geometry | |
| Bond length (Å) | 0.006 |
| Bond angle (°) | 1.2 |
| R factor (%) (reflections)d | 22.4 [60,614] |
| Rfree (%) (reflections)e | 26.7 [6,090] |
a
ESRF, European Synchrotron Radiation Facility.
b
Data for the highest-resolution shell are given in parentheses.
c
Rsym = Σ|I − 〈I〉|ΣI, where I is the intensity of the individual reflections and 〈I〉 is the mean intensity over symmetrically equivalent reflections.
d
R = Σ‖Fobs| − |Fcalc‖IΣ|Fobs|, where Fobs and Fcalc are the observed and calculated structure factor amplitudes, respectively.
e
Rfree is the same calculation including only the randomly chosen 10% of reflections not used for refinement.