Table 2.
Data Collection and Refinement Statistics
| Fab JR4-ID1 | Fab A32-ID2293 HEK Cells | Fab A32-ID2E. coli | |
|---|---|---|---|
| Data Collection | |||
| Wavelength (Å) | 0.9795 | 1.128 | 0.9795 |
| Space group | C222(1) | P2(1)2(1)2 | P2(1)2(1)2 |
| Cell parameters | |||
| a, b, c (Å) | 78.5, 89.9, 180.8 | 75.7, 208.2, 73.2 | 75.8, 211.8, 72.9 |
| α, β, γ (°) | 90, 90, 90 | 90, 90, 90 | 90, 90, 90 |
| Complexes (a.u.) | 1 | 2 | 2 |
| Resolution (Å) | 50–1.85 (1.88–1.85) | 50–3.10 (3.15–3.10) | 50.0–3.00 (3.05–3.00) |
| No. of reflections | |||
| Total | 299,100 | 165,660 | 119,799 |
| Unique | 51,569 | 19,959 | 20,655 |
| Rmergea (%) | 10.7 (100) | 18.6 (95.5) | 16.3 (88.0) |
| I/σ | 15.0 (1.1) | 14.6 (1.3) | 9.5 (1.2) |
| Completeness (%) | 94.9 (91.4) | 93.2 (96.8) | 87.1 (86.7) |
| Redundancy | 5.8 (5.7) | 8.3 (8.3) | 5.8 (5.8) |
| Refinement Statistics | |||
| Resolution (Å) | 50–1.85 | 50–3.1 | 50–3.02 |
| Rb (%) | 18.6 | 23.2 | 22.7 |
| Rfreec (%) | 22.3 | 28.9 | 28.8 |
| No. of atoms | |||
| Protein | 4,034 | 8,470 | 8,600 |
| Water | 376 | 0 | 4 |
| Ligand/ion | 32 | 0 | 0 |
| Overall B value (Å2) | |||
| Protein | 44.7 | 95.8 | 90.2 |
| Water | 42.4 | – | 61.7 |
| Ligand/ion | 47.5 | – | – |
| RMSD | |||
| Bond lengths (Å) | 0.018 | 0.010 | 0.008 |
| Bond angles (°) | 1.79 | 1.53 | 1.45 |
| Ramachandrand | |||
| Favored (%) | 8.9 | 87.5 | 87.0 |
| Allowed (%) | 8.9 | 9.4 | 9.4 |
| Outliers (%) | 0.5 | 3.1 | 3.6 |
| PDB | 5FCU | 4YBL | 4YC2 |
Values in parentheses are for highest-resolution shell.
a
Rmerge = ∑|I − <I>|/∑I, where I is the observed intensity and <I> is the average intensity obtained from multiple observations of symmetry-related reflections after rejections.
b
R = ∑‖Fo| − |Fc‖/∑|Fo|, where Fo and Fc are the observed and calculated structure factors, respectively.
c
Rfree as defined by Brünger (1992).
d
Calculated with MolProbity.