TABLE 1.
Summary of crystallographic analysis
| Type of statistic | Result |
|---|---|
| Data collection | |
| Resolution (Å) | 25.0–1.8 |
| No. of reflections (total/unique) | 40,562/11,590 |
| Completeness (%) | 99.6 (99.5)b |
| Rsym (%)a | 5.1 (10.9)b |
| Signal (<I/ςI>) | 16.5 |
| Refinementc | |
| Resolution (Å) | 25.0–1.8 |
| No. of reflections | 11,488 |
| Rcryst/Rfree (%)d | 19.4/20.7 |
| rms deviations | |
| Bonds (Å) | 0.005 |
| Angles (°) | 1.31 |
| B-factors (Å2)e | 1.00 |
a
Rsym = 100 × ΣhklΣi|li(hkl) − <l(hkl)>|/ΣhklΣi li(hkl).
b
Value in parentheses is for the highest-resolution shell: 1.86 − 1.8 Å.
c
Atomic model: 994 protein atoms, 3 SO42− ions, and 96 water molecules.
d
Rcryst/free = 100 × Σhkl ∥Fo(hkl)|−|Fc(hkl)∥ / Σhkl|Fo(hkl)|, where Fo (>0ς) and Fc are the observed and calculated structure factors, respectively. Five percent of the reflections were used for calculation of Rfree.
e
B-factors for bonded protein atoms.