Table 1.
Summary of crystallographic analysis
| Diffraction dataa | |
| Resolution (Å) | 1.40 (1.45-1.40) |
| Measured reflections | 85538 |
| Unique reflections | 17050 (811) |
| Completeness (%) | 86.8 (42.3) |
| Average I/σ | 24.5 (4.1) |
| Rmerge (%)b | 4.2 (19.5) |
| Refinement | |
| Resolution range (Å) | 50.0-1.40 (1.46-1.40) |
| R-factor/Rfree (%)c | 19.7/21.6 (29.8/32.0) |
| Number of protein atoms | 559 |
| Number of ions | 1 acetate, 2 BME, 2 Cl- |
| Number of water molecules | 147 |
| RMSD | |
| Bond lengths | 0.006 Å |
| Bond angles | 1.29° |
| Dihedrals | 24.12° |
| Improper | 0.70° |
a
Numbers enclosed in parentheses are the values of the highest resolution shell.
b
Rmerge = Σ|I − 〈I〉|/〈ΣI〉 where I and are the measured and averaged intensities of multiple measurements of the same reflection. The summation is over all the observed reflections.
c
R-factor = Σ∥Fo| −|Fc∥/Σ|Fo|, where Fo denotes the observed structure factor amplitude and Fc denotes the structure factor calculated from the model.