Table 1.
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 single crystal was used for the data collection.
Values in parentheses are for the highest-resolution shell.
Rsym = Σh|Ih – <I>|/ΣhIh, where Ih and <I> represent the diffraction intensity values of individual measurements and the corresponding mean values, respectively.
Rwork = (Σh||Fo| – |Fc||)/Σh|Fo|, where Fo and Fc are observed and calculated structure factor amplitudes, respectively.
Rfree was calculated for 5% of the randomly selected reflections of the data set that were not used in the refinement.