Table 2.
Crystallographic Data Collection and Refinement Statistics
| data collection | APS-14ID-B |
|---|---|
| λ (Å) | 1.000 |
| Space group | P22121 |
| Cell dimensions | |
| a, b, c (Å) | 97.3, 119.2, 127.8 |
| α, β, γ (deg) | 90.0, 90.0 90.0 |
| Resolution (Å)a | 97.33–1.64 (1.69–1.64) |
| R meas a,b | 0.116 (0.506) |
| R pim a,c | 0.077 (0.431) |
| I/σ(I)a | 12.1 (1.0) |
| CC1/2 (%) | 98.2 (75.1) |
| Completeness | 98.8 (91.4) |
| Total/unique reflections | 1 012 426/179 842 |
| Multiplicity | 5.6 (2.1) |
| Z (molecules/ASU)d | 7 |
| Refinement | |
| Rwork/Rfreee,f | 23.7/28.2 |
| No. atoms (non-hydrogens) | 10 544 |
| Protein | 9775 |
| Ligand | 65 |
| Water | 704 |
| Average B (Å2) | 31.8 |
| Protein (Å2) | 31.2 |
| ACP1-06 (Å2) | 62.6 |
| Waters (Å2) | 36.7 |
| RMSD Bonds (Å) | 0.012 |
| RMSD Angles (deg) | 1.28 |
| Ramachandran favored (%) | 98.0 |
| Ramachandran allowed (%) | 1.7 |
| Ramachandran outliers (%) | 0.3 |
| No. of TLS groups | 1 |
| Clashscore | 6.76 |
| PDB code | 6W9T |
a
Values in parentheses are for highest-resolution shell.
b
Rmeas: Multiplicity-independent R factor = Σhkl [Nhkl/(Nhkl − 1)]1/2 Σi | Ii(hkl) – 〈I(hkl)〉|/Σhkl Σi Ii(hkl).
c
Rpim: Precision indicating merging R factor = Σhkl [1/(Nhkl − 1)]1/2 Σi |Ii(hkl) – 〈I(hkl)〉|/Σhkl Σi Ii(hkl).
d
Za: Number of ClpP subunits in the asymmetric unit.
e
Rwork: = Σ ‖Fobs| – |Fcalc‖/Σ |Fobs|, where Fcalc and Fobs are the calculated and observed structure factor amplitudes, respectively.
f
Rfree: Statistic is the same as Rwork except calculated on 5% of the total reflections chosen randomly and omitted from the refinement.