Table I. X-ray diffraction data collection and refinement statistics.
| Data collection |
|
| Resolution (Å) | 20.0–2.5 |
| Measured reflections | 570 918 |
| Unique reflections | 33 852 |
| Completeness (%, > –1σ)a | 97.7 (96.0) |
| Rsym (%)a,b | 5.3 (46.4) |
| Average I/σ(I)a |
19.47 (1.9) |
| Refinement |
|
| Rworkc | 0.260 |
| Rfreec | 0.302 |
| Number of reflections [F > 2σ (F)] | 28 067 |
| Number of protein atoms | 5549 |
| Number of non-protein atoms | 337 |
| R.m.s.d.d bond length (Å) | 0.009 |
| R.m.s.d.d bond angles (°) | 1.47 |
| Average B-factors (Å2, main chain/side chain) | 61.5/62.3 |
| Ramachandran analysis most favored/allowed | 82.8/17.2 |
aLast shell (2.59–2.5 Å resolution) value is in parentheses.
bRsym = Σhkl[Σi|Ihkl,i – <Ihkl>|]/Σhkl,i<Ihkl>, where Ihkl,i is the intensity of an individual measurement of the reflection with Miller indices h, k and l, and <Ihkl> is the mean intensity of the reflection.
cRwork = Σ||Fobs| – |Fcalc||/Σ|Fobs|, where Fobs and Fcalc are observed and calculated structure factor amplitudes. Rfree is equivalent to Rwork, except 5% of total reflections were set aside to test the progress of refinement.
dR.m.s.d., root mean square deviation from ideal geometry.