TABLE 3.
Summary of crystallographic analysis
| Data collection statistics
|
Refinement statisticsc
|
|||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| Resolution (Å) | Reflections (total/unique) | Completeness (%) | Rsyma (%) | Signal (〈I/σI〉) | Resolution (Å) | Reflections | Rcryst/Rfreed (%) | Root-mean-square deviations
|
||
| Bonds (Å) | Angles (degrees) | B factorse (Å2) | ||||||||
| 30-2.8 | 179,609/15,732 | 96.7 (100)b | 6.3 (26.8)b | 26.9 | 25-2.8 | 15,252 | 25.3/28.8 | 0.014 | 1.64 | 64 |
a
Rsym = 100 × ΣhklΣI|II(hkl) − 〈I(hkl)〉| ΣhklΣIII(hkl).
b
Value in parentheses is for the highest resolution shell: 2.9 to 2.8 Å.
c
Atomic model: 2,678 protein atoms, 1 PEG-400 molecule, and 2 sulfate ions.
d
Rcryst/free = 100 × hkl Fo(hkl)| |Fc(hkl)/hkl |Fo(hkl)|, where Fo (>0) and Fc are the observed and calculated structure factors, respectively. Ten percent of the reflections were used for calculation of Rfree.
e
For bonded protein atoms.