Table 1.
Crystallographic Data and Refinement Statistics
| Data Collection | |
| Wavelength (Å) | 0.980377 |
| Space group | P212121 |
| Cell dimensions: a, b, c (Å) | 62.3, 66.5, 138.9 |
| Resolution (Å) | 20.0–2.00 (2.07–2.00) |
| # Reflections: Measured/Unique | 68,739 (4,858)/10,919 (1,278) |
| Completeness (%) | 92.3 (64.9) |
| Mean redundancy | 6.3 (3.8) |
| <I/σI> | 16.7 (3.9) |
| Rsym a | 0.09 (0.278) |
| Refinement | |
| Resolution (Å) | 20.0–2.00 (2.05–2.00) |
| Rb/Rfree (%)c | 18.3 (22.3)/21.0 (28.7) |
| # Reflections, R/Rfree | 34,474 (1,525)/1,960 (79) |
| Total atoms: Protein/Water | 3,912/385 |
| Stereochemical ideality (rmsd): Bonds/ Angles (Å/°) | 0.014/1.15 |
| Mean B-factors (Å2): Overall/Protein/ Water | 34.8/34.1/41.3 |
| Ramachandran Analysis: Favored/ Allowed (%) | 99.2/0.8 |
a
Rsym = Σ h Σ i|Ii(h) − < l(h) >|/Σ h Σ iIi(h) where Ii(h) is the integrated intensity of the ith reflection with the Miller Index h and <I(h)> is the average over Friedel and symmetry equivalents.
b
R value = Σ (|Fobs| − k|Fcalc|)/Σ |Fobs|.
c
Rfree is calculated using a 5% subset of the data that are removed randomly from the original data and excluded from refinement.