TABLE 2.
Data collection and refinement statistics
| Parameter | Value |
|---|---|
| Data collection | |
| Space group | P 31 2 1 |
| Cell constants (Å) | a = b = 109.42, c = 184.46 |
| Wavelength (Å) | 0.978 |
| No. of measurements | 88,939 |
| No. of unique reflections | 26,635 |
| Resolution range (Å) | ∞-2.85 |
| Completeness (%)a | 88.2 (67.2) |
| Rmerge (%)a,b | 0.124 (0.45) |
| <I/σ(I)>a | 8.16 (2.62) |
| Refinement | |
| Resolution range used for refinement (Å) | 30.0-2.85 |
| No. of reflections used | 25,260 |
| Crystallographic Rfactor (free Rfactor)c | 0.258 (0.287) |
| No. of solvent molecules | 46 |
| R.m.s. deviation from target values | |
| Bonds (Å) | 0.010 |
| Angles (°) | 1.49 |
| Avg temp factor, protein atoms (Å2) | 45.3 |
| Avg temp factor, Fe atoms (Å2) | 45.4 |
a
The values in parenthesis indicate the outermost 3.07 to 2.85-Å resolution shell.
b
Rmerge = ΣhklΣi|Ii(hkl) − <I(hkl)>|/ΣhklΣiIi(hkl), where Ii is the ith measurement of reflection I (hkl).
c
Rfactor = Σhkl||Fobs| − k |Fcalc||/Σhkl |Fobs|. The free Rfactor is the same for a test set of 5% reflections not used during refinement.