Table 1.
X-ray data collection and refinement statistics
| Data collection | |
| Resolution (Å) | 50–2.3 |
| Observations | 73 243 |
| Unique reflections | 18 251 |
| Redundancy | 4.0 |
| Completenessa (%) | 97.5 (99.2) |
| Rsyma,b (%) | 7.8 (39.4) |
| <I/σI>a | 12.3 (2.1) |
| Refinementc | |
| Resolution (Å) | 50–2.3 |
| Reflections | 17 319 |
| Rcrystd/Rfree (%) | 19.7/23.5 |
| r.m.s.d. bond lengths (Å) | 0.010 |
| r.m.s.d. bond angles (deg) | 1.29 |
| Average B-factors (Å2) | |
| All atoms | 34.2 |
| IGF1RK | 34.3 |
| PQIP | 21.6 |
| Solvent | 35.1 |
| aValue in parentheses is for the highest resolution shell: 2.38–2.30 Å. | |
| bRsym=100 × ∑∣I–〈I〉∣/∑I. | |
| cAtomic model includes 2324 protein atoms, 37 PQIP atoms, 1 Ca2+ and 165 water molecules. | |
| dRcryst=100 × ∑∣∣Fo∣–∣Fc∣∣/∑∣Fo∣, where Fo and Fc are the observed and calculated structure factors, respectively (Fo>0σ). Rfree was determined from 5% of the data. | |