Table 2 RPC5-tWHD1 (aa. 259–440) data collection, phasing and refinement statistics for MAD (SeMet) structures.
Crystal 1 (Native) | Crystal 2 (SeMet) | |||
|---|---|---|---|---|
Data collection | ||||
Space group | P6122 | P6122 | P6122 | P6122 |
Cell dimensions | ||||
a, b, c (Å) | 56.30, 56.30, 275.88 | 56.43, 56.43, 277.27 | 56.44, 56.44, 277.17 | 56.41, 56.41, 276.95 |
α, β, γ (°) | 90, 90, 120 | 90, 90, 120 | 90, 90, 120 | 90, 90, 120 |
Peak | Inflection | Remote | ||
Wavelength | 0.91983 | 0.97965 | 0.97980 | 0.971970 |
Resolution (Å) | 48.01–2.23 (2.29–2.23) | 48.87–2.72 (2.79–2.72) | 48.88–2.63 (2.70–2.63) | 48.11–2.50 (2.56–2.50) |
Rsym or Rmerge | 0.05 (0.749) | 0.324 (2.163) | 0.268 (1.820) | 0.246 (1.656) |
I/σI | 26.9 (5.7) | 8.7 (1.5) | 9.4 (1.5) | 8.7 (1.2) |
Completeness (%) | 100.0 (100.0) | 100.0 (100.0) | 100.0 (100.0) | 100.0 (100.0) |
Redundancy | 27.4 (28.8) | 21.6 (19.6) | 21.2 (15.8) | 20.0 (10.6) |
Refinement | ||||
Resolution (Å) | 45.97–2.23 (2.31–2.23) | |||
No. reflections | 376,023 | |||
Rwork/Rfree | 0.1800/0.2193 | |||
No. of atoms | 1496 | |||
Protein | 1371 | |||
Ligand/ion | 4 | |||
Water | 121 | |||
B-factors | ||||
Protein | 50.52 | |||
Ligand/ion | 89.50 | |||
Water | 54.85 | |||
R.m.s deviations | ||||
Bond lengths (Å) | 0.008 | |||
Bond angles (°) | 0.84 | |||
