Table 1.
X-ray data collection and refinement statistics (molecular replacement)
| AgrACa | |
|---|---|
| Data collection | |
| Space group | P212121 |
| Cell dimensions | |
| a, b, c (Å) | 41.4, 45.9, 112.1 |
| α, β, γ (°) | 90.0, 90.0, 90.0 |
| Resolution range (Å) | 25.00-1.52 (1.55-1.52)b |
| Rsymc | 0.045 (0.563) |
| I/σ(I) | 32.9 (2.0) |
| Completeness (%) | 97.2 (89.8) |
| Redundancy | 3.3 (2.7) |
| Refinement | |
| Resolution (Å) | 20.72-1.52 |
| No. reflections | 31964 |
| Data cutoff | σ(F) > 0 |
| Rworkd/Rfreee | 0.180/0.209 |
| No. atoms per asymmetric unit | |
| Protein | 1702 |
| Glycerol | 18 |
| Water | 254 |
| Average B-factors (A2) | |
| Protein | 20.5 |
| Glycerol | 32.3 |
| Water | 32.6 |
| Rms deviations from ideality | |
| Bond lengths (Å) | 0.006 |
| Bond angles (°) | 1.048 |
a
A single crystal was used for the data collection.
b
Values in parentheses are for the highest-resolution shell.
c
Rsym = Σh|Ih – <I>|/ΣhIh, where Ih and <I> represent the diffraction intensity values of individual measurements and the corresponding mean values, respectively.
d
Rwork = (Σh||Fo| – |Fc||)/Σh|Fo|, where Fo and Fc are observed and calculated structure factor amplitudes, respectively.
e
Rfree was calculated for 5% of the randomly selected reflections of the data set that were not used in the refinement.