Table 1 Data collection and refinement statistics.
From: Engineering protein assemblies with allosteric control via monomer fold-switching
Classical geometry (condition a) | Domain swapping (condition b) | |
|---|---|---|
Data collection | ||
Space group | P622 | P622 |
Cell dimensions | ||
a, b, c (Å) | 68.77, 68.77, 50.56 | 68.55, 68.55, 53.10 |
α, β, γ (°) | 90, 90, 120 | 90, 90, 120 |
Resolution (Å) | 34.39–1.50 (1.55–1.50) | 39.58–1.65 (1.71–1.65) |
Rmerge | 0.059 (2.059) | 0.083 (1.195) |
I /σI | 23.00 (1.80) | 15.20 (1.60) |
Completeness (%) | 99.50 (99.65) | 99.84 (99.23) |
Redundancy | 18.1 (18.3) | 8.3 (8.3) |
Refinement | ||
Resolution (Å) | 34.39–1.50 (1.55–1.50) | 39.58–1.65 (1.71–1.65) |
No. of reflections | 11,750 (1143) | 9305 (903) |
Rwork/Rfree | 0.21 (0.35)/0.26 (0.37) | 0.18 (0.27)/0.22 (0.34) |
No. of atoms | ||
Protein | 527 | 529 |
Ligand/ion | – | – |
Water | 65 | 97 |
B-factors | ||
Protein | 37.53 | 26.38 |
Ligand/ion | – | – |
Water | 43.44 | 37.83 |
R.m.s. deviations | ||
Bond lengths (Å) | 0.006 | 0.006 |
Bond angles (°) | 0.86 | 0.86 |
