Table 3.
Data Collection and Refinement Statistics
| Crystal Parameters | |
| Space group | P43212 |
| a,b,c (Å) | 72.0, 72.0, 262.6 |
| Data Collection Statistics | |
| Wavelength (Å) | 1.5418 |
| Resolution (Å) | 32.2 – 2.4 (2.5 – 2.4)a |
| Total Reflections | 247952 (28360) |
| Unique reflections | 26680 (2605) |
| Rmergeb | 0.105 (0.44) |
| Mean (I)/σ (I) | 10.4 (5.1) |
| Completeness (%) | 99.6 (100.0) |
| Redundancy | 9.3 (10.9) |
| Refinement Statistics | |
| Protein molecules (chains) in A.U. | 2 |
| Residues | 432 |
| Inhibitors | 2 |
| Water molecules | 57 |
| Total number of atoms | 3617 |
| Rcrystc/Rfreed (%) | 24.5/26.5 |
| Average B-factor (Å2) (all atoms) | 56.5 |
| Rmsd on angles (°) | 1.098 |
| Rmsd on bonds (Å) | 0.007 |
a
The data collection statistics in brackets are the values for the highest resolution shell.
b
Rmerge = ΣhklΣi|Ii (hkl)-〈I(hkl)〉|/ΣhklΣiIi(hkl) where Ii (hkl) is the intensity of an individual reflection and 〈I(hkl)〉 is the mean intensity of that reflection.
c
Rcryst = Σhkl||Fobs| − |Fcalc||/Σhkl|Fobs| where Fobs and Fcalc are the observed and calculated structure-factor amplitudes, respectively.
d
Rfree is calculated using 5% of the reflections randomly excluded from refinement.