Table 1. Crystallographic statistics.
Values in parentheses are for the highest resolution shell.
| Data collection | |
| Space group | P41212 |
| Unit-cell parameters | |
| a () | 70.525 |
| b () | 70.525 |
| c () | 71.517 |
| Wavelength () | 1.0809 |
| Resolution () | 31.541.90 |
| No. of unique reflections | 13866 |
| R merge † | 4.0 (42.1) |
| I/(I) | 37.3 (2.6) |
| Completeness (%) | 98.8 (93.4) |
| Multiplicity | 6.7 (3.5) |
| Refinement | |
| Resolution () | 31.541.90 |
| No. of reflections | 13866 |
| R work/R free ‡ (%) | 18.0/24.5 |
| Total No. of atoms | 1361 |
| No. of protein atoms | 1171 |
| Waters | 190 |
| B factors (2) | |
| Average | 29.37 |
| Protein | 27.65 |
| Solvent | 39.96 |
| R.m.s. deviations§ | |
| Bond lengths () | 0.018 |
| Bond angles () | 1.890 |
| Ramachandran plot | |
| Favored regions (%) | 91.0 |
| Allowed regions (%) | 9.0 |
| Outliers (%) | 0 |
†
R
merge = 
, for i observations of the intensity I(hkl) of reflection hkl.
‡
R = 
. R
free was calculated using 5% of the data, which were omitted from refinement.
§
Bond and angle deviations from ideal values.