Table 1.
Crystallographic data collection and refinement statistics.
| MET - 107_A07 Fab complex | |
|---|---|
| Data collection | |
| Radiation Source, Beamline | ESRF, ID29 |
| Wavelength (Å) | 0.91376 |
| Space group | P22121 |
| Cell dimensions | |
| a, b, c (Å) | 71.88 82.28 267.30 |
| α, β, γ (°) | 90, 90, 90 |
| Resolution (Å) | 48.95–2.60 (2.74–2.60)1 |
| Rmeas 2 | 11.1 (88.3) |
| <I/σ(I)> | 11.7 (2.0) |
| Completeness (%) | 99.0 (95.8) |
| Redundancy | 5.5 (5.5) |
| No. of unique reflections | 49,099 (6,685) |
| Refinement | |
| Resolution (Å) | 48.94–2.60 |
| No. of reflections: | |
| Total | 48,940 |
| Rfree set | 2,000 |
| Rcryst 3/Rfree 4 | 21.5/25.7 |
| Contents of asymmetric unit: | |
| Protein atoms | 10,043 |
| Solvent atoms | 88 |
| R.m.s deviations: | |
| Bond lengths (Å) | 0.005 |
| Bond angles (°) | 0.999 |
1The statistics shown in parentheses are for the highest-resolution shell.
2 R meas = (Σ hkl [N/(N-1)]1/2 Σ i |I i(hkl)−I mean(hkl)|)/Σ hkl Σ i I i(hkl), where N is redundancy.
3 R cryst = Σ hkl ||Fobs(hkl)|−|Fcalc(hkl)||/Σ hkl |Fobs(hkl)|.
4 R free is the same as R cryst for a random subset not included in the refinement of about 4% of total reflection.