Table 1.
X-ray data collection and refinement statistics.
| Space group | Orthorhombic – P212121 |
| Cell dimensions | a = 38.4 Å; b = 54.7 Å; c = 94.7 Å |
| Resolution range (Å) | 50–1.76 |
| Rsymma (outer shell) | 0.082 (0.299) |
| I/σI (outer shell) | 14.5 (2.9) |
| Completeness (outer shell) % | 91.9 (65.8) |
| Total number of reflections | 230,027 |
| Number of unique reflections | 20,481 |
| Redundancy (outer shell) | 4.8 (2.5) |
| Wilson B-factor (Å2) | 29.0 |
| Rcrystb/Rfreec | 0.239/0.285 |
| Average B-factor (Å2) | |
| Overall | 34.7 |
| Protein (chain A, B) | 33.6, 35.5 |
| Chloride ion | 36.9 |
| Solvent | 37.1 |
| RMS deviation | |
| Bond length (Å) | 0.007 |
| Bond angle (°) | 1.012 |
| Ramachandran plot statistics | |
| Favoured (%) | 97.71 |
| Additional favoured (%) | 2.29 |
| PDB ID | 4B36 |
a
Rsymm = Σh Σi |I(h) − Ii(h)|/Σh ΣiIi(h), where Ii(h) and I(h) are the ith and the mean measurements of the intensity of reflection h, respectively.
b
Rcryst = Σh |Fo − Fc|/ΣhFo, where Fo and Fc are the observed and calculated structure factor amplitudes of reflection h, respectively.
c
Rfree is equal to Rcryst for a randomly selected 5.0% subset of reflections not used in the refinement.