TABLE 2.
Data collection, phasing, and refinement statistics
| Parametera | Peak | Remote |
|---|---|---|
| Data collection | ||
| Wavelength (Å) | 0.980301 | 0.95 |
| No. of measured reflections | 317,815 | 322,971 |
| No. of unique reflections | 45,717 | 45,900 |
| Redundancy | 6.95 (5.80) | 7.04 (6.64) |
| Resolution (Å)b | 30.86-2.00 (2.07-2.00) | 28.26-2.00 (2.07-2.00) |
| Rmergec (%)b | 6.2 (52.8) | 6.1 (59.7) |
| Completeness (%)b | 99.6 (97.7) | 99.8 (100) |
| Average I/σ(I)b | 10.9 (2.4) | 10.7 (2.0) |
| Phasing | ||
| Phasing power | 1.96 | |
| Figure of merit | 0.374 | |
| Figure of merit after solvent flattening | 0.938 | |
| Refinement | ||
| Protein atoms | 3,574 | |
| Water molecules | 317 | |
| R/Rfree (%)d | 20.9/24.8 | |
| Mean B-factor (Å2) | 47.63 | |
| RMS deviation from ideal | ||
| Bond length (Å) | 0.01 | |
| Bond angles (°) | 1.36 | |
| Residues in Ramachandran plot (%)e | ||
| Favored | 95.9 | |
| Allowed | 4.1 | |
| Outliers | 0 | |
| Estimated coordinate errorf | 0.34 |
a
Space group, P21212; unit cell dimensions (Å, °), a = 137.2, b = 69.1, c = 70.2, α = β = γ = 90.0.
b
Values in parentheses are for the outer resolution shell, 2.07 to 2.00 Å.
c
Rmerge = ∑I−<I>/∑I, where I is the measured intensity for symmetry-related reflections and <I> is the mean intensity for the reflection.
d
Rcryst = ∑(Fobs−Fcalc)/∑(Fobs); Rfree is Rcryst for the 5% cross-validated test data.
e
According to the Ramachandran plot in PROCHECK (31).
f
Calculated using the method of Read (47).