Table I. Data collection and statistics of crystallographic data and refinement.
| Data sets | BM14 | ID14-EH2 | ID14-EH4 |
|---|---|---|---|
| Wavelength (Å) | 0.96 | 0.93 | 0.93 |
| Resolution (last shell) (Å) | 15–3.2 (3.3–3.2) | 40–2.8 (2.9–2.8) | 15–2.5 (2.6–2.5) |
| Total reflections | 46 568 | 71 272 | 87 788 |
| Unique reflections | 8871 | 14 441 | 22 453 |
| Redundancy | 5.2 | 4.9 | 3.9 |
| Completeness (last shell) (%) | 99.6 (99.2) | 96.8 (99.5) | 98.9 (95.5) |
| Rsym (last shell) (%) | 5.3 (25.4) | 7.4 (24.9) | 4.5 (19.4) |
|
I/σ (last shell) |
30.6 (6.5) |
18.2 (8.8) |
22.7 (5.3) |
| Refinement statistics | |||
| Reflections in working set (95% at 2σ) | 19 261 | ||
| Reflections in test set (5% at 2σ) | 981 | ||
| Rcrysta (%) | 22.5 | ||
| Rfreeb (%) | 25.7 | ||
| R.m.s.d. bonds (Å) | 0.011 | ||
| R.m.s.d. angles (°) | 1.50 | ||
| R.m.s.d. between monomers 1 and 2 (Å) | 0.046 | ||
| Monomers 1 and 2 | |||
| non-hydrogen protein atoms | 1766 and 1707 | ||
| non-hydrogen ligand atoms | 22 and 22 | ||
| solvent molecules | 127 and 78 | ||
| Average B factor (Å2) | |||
| non-hydrogen protein atoms | 47.2 and 57.9 | ||
| non-hydrogen ligand atoms | 41.7 and 48.2 | ||
| solvent molecules | 58.3 and 62.8 | ||
R.m.s.d is the root mean square deviation from ideal geometry.
aRsym = Σhkl Σi |Ihkl,i – <Ihkl,i>|/Σhkl Σi |Ihkl,i| where <Ihkl,i> is the average intensity of the multiple hkl,i observations for symmetry-related reflections.
bRcryst = Σ|Fobs – Fcalc|/Σ|Fobs|, where Fobs and Fcalc are observed and calculated structure factors. Rfree is calculated from a randomly chosen 5% of reflections (2σ) and Rcryst is calculated for the remaining 95% of reflections (2σ).