Table 2 Data collection and refinement statistics (molecular replacement).
From: Activation of Xer-recombination at dif: structural basis of the FtsKγ–XerD interaction
XerDC-FtsKγ | |
|---|---|
Data collection | |
Space group | P 65 |
Cell dimensions | |
a, b, c (Å) | 83.44, 83.44, 88.66 |
α, β, γ (°) | 90, 90, 120 |
Resolution (Å) | 56.02–2.30 (2.38–2.30)* |
R merge | 0.12 (1.66) |
R pim | 0.04 (0.54) |
CC(1/2) | 1.00 (0.53) |
I/σI | 13.8 (2.1) |
Completeness (%) | 100 (100) |
Redundancy | 11.0 (11.2) |
Refinement | |
Resolution (Å) | 36.13 - 2.3 (2.38–2.30) |
No. reflections | 15639 (1566) |
Rwork/Rfree | 0.191 (0.287)/0.229 (0.303) |
CC work | 0.84 (0.65) |
CC free | 0.85 (0.78) |
CC* | 0.94 (0.80) |
No. atoms | 1976 |
Protein | 1915 |
Ligand/ion | — |
Water | 61 |
B-factors | Overall 67.5 |
Protein | 67.9 |
Ligand/ion | — |
Water | 52.6 |
R.M.S. deviations | |
Bond lengths (Å) | 0.01 |
Bond angles (°) | 1.16 |
