|
Data collection and refinement statistics |
|
| tteRBP |
|
|
|
|
| Data Collection |
|
| Detector Type |
Mar225 |
| Wavelength (Å) |
1.0 |
| Resolution (Å) |
15.0–1.9 |
| Measured reflections |
123829 |
| Unique reflections |
16732 |
| Mean I/σ(I)a |
11.6 (4.1) |
| Completeness (%)a |
96.0 (95.1) |
| Rsym (%)a,b |
8.0 (32.4) |
| Redundancya |
3.3 (3.1) |
| Refinement |
|
| Resolution (Å) |
15.0–1.9 |
| Num. of Reflections (working set/test set) |
35702/1890 |
| Rcrystc |
19.9 (26.0) |
| Rfreed |
23.4 (30.6) |
| Number of atoms |
|
| Protein |
4265 |
| Water |
346 |
| Ligand |
20 |
| r.m.s.d. |
|
| Bond lengths (Å) |
0.011 |
| Bond angles (°) |
1.221 |
| Average B-factor (Å2) |
|
| Main Chain |
17.8 |
| Side Chain |
22.7 |
| Solvent |
28.7 |
| Ligand |
10.1 |
| Protein Geometry |
|
| Ramachandran outliers (%) |
0.55 |
| Ramachandran favored (%) |
98.7 |
| Rotamer outliers (%) |
0.47 |
|
aNumber in parentheses represent values in the highest resolution shell. bRsym = ∑|(I-<I>)|/(∑I), where <I> is the average intensity of multiple measurements. cRcryst = ∑|Fobs-Fcalc|/(∑|Fobs|) dRfree is the R-factor based on 5% of the data excluded from refinement. | |
Cuneo et al. BMC Structural Biology 2008 8:20 doi:10.1186/1472-6807-8-20 |
|