Table 1.
Data collection and refinement statistics
| Con-Ins-G1-bound Fv-83-7-bound μIR PDB 6VEQ) | Human-insulin-bound Fv-83-7-bound μIR (PDB 6VEP) | Mini-Ins (PDB 6VET) | |
|---|---|---|---|
| Data collection | |||
| Space group | I222 | P21 | P212121 |
| Cell dimensions | |||
| a, b, c (Å) | 106.16, 227.12, 228.70 | 100.03, 130.12, 148.18 | 28.37, 52.12, 80.50 |
| α, β, γ (°) | 90, 90, 90 | 90, 90.27, 90 | 90, 90, 90 |
| Resolution (Å) | 48.15–3.25 (3.35–3.25)a | 48.89–2.90 (2.95–2.90) | 43.75–1.46 (1.48–1.46) |
| Rmerge | 0.259 (2.75) | 0.263 (3.64) | 0.143 (4.47) |
| I/σ(I) | 6.4 (0.59) | 5.7 (0.44) | 9.7 (0.6) |
| CC1/2 | 0.992 (0.163) | 0.984 (0.112) | 0.999 (0.380) |
| Completeness (%) | 99.8 (99.9) | 99.0 (97.9) | 99.5 (90.4) |
| Redundancy | 5.8 (6.0) | 3.8 (3.6) | 13.0 (12.5) |
| Refinement | |||
| Resolution (Å) | 48.15–3.25 | 48.89–2.90 | 43.75–1.46 |
| No. reflections | 43845 | 82572 | 21302 |
| Rwork / Rfree | 0.228 / 0.277 | 0.193 / 0.225 | 0.201 / 0.238 |
| No. atoms | |||
| Protein | 9247 | 19300 | 1953 |
| Ions | 20 | 0 | 0 |
| Water | 0 | 18 | 119 |
| B factors | |||
| Protein | 124 | 102 | 32 |
| Ions | 127 | - | - |
| Water | - | 66 | 38 |
| R.m.s. deviations | |||
| Bond lengths (Å) | 0.002 | 0.010 | 0.006 |
| Bond angles (°) | 0.5 | 1.2 | 0.6 |
a
Values in parentheses are for highest-resolution shell. All diffraction data sets were collected from a single respective crystal