Table 1.
Crystallographic data collection and model refinement statistics for ED1
| Data Collection | |
| Wavelength [Å] | 1.54184 |
| Frames/Runs | 1148/4 |
| Rotation [°] | 360 |
| Space group | P 21 |
| Unit cell dimensions | |
| a, b, c [Å] | 39.060(2), 95.631(3), |
| α, β, γ [˚] | 40.916(3), |
| 90.0, 108.576(8), 90.0 | |
| Resolution [Å] | 95.63 – 1.99 |
| (2.06 – 1.99) a) | |
| Rint b) | 0.111 (0.216) |
| I/σ(I) | 14.6 (2.6) |
| Completeness [%] | 97.0 (94.3) |
| Average redundancy | 3.8 (3.5) |
| Structure refinement | |
| Resolution range [Å] | 17.87‐1.99 |
| No. unique reflections | 18 932 |
| R work c) /R free d) | 0.262/0.292 |
| Number of atoms | |
| Protein | 2670 |
| Ligand/ions | 4 |
| Water | 277 |
| Avg. B‐factor | |
| Protein | 20.04 |
| Ligand/ions | 22.7 |
| Water | 20.3 |
| RMS deviations e) | |
| Bond lengths [Å] | 0.002 |
| Bond angles [°] | 0.44 |
| Ramachandran plot f) | |
| favored [%] | 93.8 |
| allowed [%] | 4.5 |
| outliers [%] | 2.4 |
a)
The highest resolution shell is shown in parenthesis
b)
Rint = ∑hkl∑i|Ii(hkl) − <I(hkl)> /∑hkl∑iIi(hkl), where Ii(hkl) is the intensity of an observation and is the mean value for its unique reflection. Summations are over all reflections
c)
Rwork = ∑h|Fo(h)‐Fc(h)|/∑hFo(h), where Fo and Fc are the observed and calculated structure factor amplitudes, respectively.
d)
Rfree was calculated with 5% of the data excluded from the refinement.
e)
RMS deviation, root mean square deviation from ideal values.
f)
The categories were defined by Molprobity in PHENIX.