Table 4. Data collection parameters and refinement statistics.
| Data collection | C5685•mAChE |
| PDB entry code | 4A23 |
| Space group | P212121 |
| Unit cell dimensions (Å) | 78.9×111.8×227.0 |
| Resolution range (Å) | 19.64–2.40 (2.4–2.53) |
| Total number of reflections | 585242 (85350) |
| Unique reflections | 79036 (11407) |
| Completeness (%) | 99.6 (99.8) |
| Multiplicity | 7.4 (7.5) |
| R merge 1 | 0.053 (0.358) |
| Mean(I)/sd(I) | 25.8 (7.5) |
| Refinement | |
| R-factor2/R free 3 (%) | 17.5/20.9 |
| B-factor4 (Å2) | 48.24 |
| Number of water molecules | 871 |
| RMSD from ideal values | |
| Bond lengths (Å) | 0.008 |
| Bond angle (°) | 1.135 |
| Ramachandran plot %/no. of residues | |
| Most favoured regions | 1030 (97.2%) |
| Allowed regions | 26 (2.5%) |
| Residues in disallowed regions | 4 (0.4%)5 |
1
Rmerge = (∑|I−<I>|)/∑I, where I is the observed intensity and <I> is the average intensity obtained after multiple observations of symmetry related reflections.
2
R-factor = (∑∥Fo|−|Fc∥)/∑Fo, where Fo are observed and Fc calculated structure factors.
3
Rfree uses 2% randomly chosen reflections defined in Brunger [77].
4
B-factor is the mean factor for protein main chain A/B.
5
Corresponds to Ala 342, Ala542, Lys496 and Ser497of the B monomer.