Table 2.
X-ray data collection and refinement statistics
| Data collection | |
|---|---|
| X-ray source |
Diamond I03 |
| Wavelength (Å) |
0.97630 |
| Space group |
P21212 |
| Unit cell (Å) |
a = 140.4, b = 174.2, c = 81.7 |
| Resolution range (Å) |
30.0 – 2.50 (2.59-2.50) |
| Unique reflections |
71197 (7000) |
| Completeness (%) |
100 (100) |
| Redundancy |
12.3 (10.5) |
| Average I/σI |
14.9 (2.1) |
| Rmerge |
0.157 (−−) |
|
Refinement |
|
| Resolution range (Å) |
30.0 – 2.50 |
| No. of atoms (protein/other atoms) |
11212/323 |
| Rms bond length deviation (Å) |
0.008 |
| Rms bond angle deviation (°) |
1.2 |
| Mean B-factor (protein/other atoms[Å2]) |
38/54 |
| Residues in preferred regions (%) |
1112 (89.5) |
| Residues in allowed regions (%) |
128 (10.3) |
| Residues in disallowed regions (%) | 3 (0.2) |
aRwork and Rfree are defined by R = Σhkl||Fobs| − |Fcalc||/Σhkl|Fobs|, where h,k,l are the indices of the reflections (used in refinement for Rwork; 5%, not used in refinement, for Rfree), Fobs and Fcalc are the structure factors, deduced from measured intensities and calculated from the model, respectively.