Table 1.
Crystallographic data collection and refinement statistics
| Data collection | |
|---|---|
|
| |
| Wavelength, Ǻ | 0.98 |
| Space group | P21212 |
| Cell parameters | a=91.15 Å, b=57.99 Å, c=39.55 Å 2 |
| Molecules/a.u. | 91.15-1.93 (2.0-1.93) |
| Resolution, Åa | |
| Number of reflections | 30982 |
| Total | 16740 |
| Unique | 9.8 (37.2) |
| Rsymb, % | 14.4 (6.1) |
| I/σ | 99.4 (98.7) |
| Completeness, % | 6.2 (6.8) |
| Redundancy | |
|
| |
| Refinement statistics | |
|
| |
| Resolution, Å | 20-1.93 |
| Rcrystc, % | 19.1 |
| Rfreed, % | 24.2 |
| Number of atoms | |
| Protein | 1629 |
| Water | 133 |
| Root mean square deviation | |
| Bond lengths, Å | 0.02 |
| Bond angles, ° | 2.0 |
| Ramachandran plot | |
| Most favored region, % | 92.3 |
| Additional allowed region, % | 7.7 |
| Generously allowed region, % | 0.0 |
| Disallowed region, % | 0.0 |
| PDB code | 4EYC |
a
All data (outer shell).
b
Rsym = Σ|I − <I>|/ΣI, where I is the observed intensity and <I> is the average intensity obtained from multiple observations of symmetry-related reflections after rejections
c
Rcryst = Σ||Fo| − k| Fc||/Σ|Fo |, where Fo and Fc are the observed and calculated structure factors, respectively
d
Rfree = defined by by Brünger (91)