Table 2 Crystallographic data collection and refinement statistics (molecular replacement)
From: Structural characterisation of the fungal Pmt4 homodimer
ctPmt4-MIR domain (PDB 9FD1) | scPmt4-MIR domain (PDB 9FD0) | |
|---|---|---|
Data collection | ||
Wavelength (Å) | 0.9677 | 0.966 |
Space group | I222 | P212121 |
Cell dimensions | ||
a, b, c (Å) | 61.16, 100.63, 103.27 | 48.59, 56.77, 78.22 |
α, β, γ (°) | 90.00, 90.00, 90.00 | 90.00, 90.00, 90.00 |
Resolution (Å) | 31.90-1.22 (1.26−1.22)*# | 41.28-1.35 (1.40−1.35)* |
Total reflections | 129,741 (960) | 93,109 (9186) |
Unique reflections | 64,952 (497) | 47,974 (4721) |
Rpim | 0.026 (0.506) | 0.038 (0.336) |
Mean I / σI | 22.83 (1.22) | 10.78 (2.32) |
CC1/2 | 0.995 (0.685) | 0.999 (0.529) |
Completeness (%) | 68.62 (5.29) | 99.43 (99.56) |
Multiplicity | 2.0 (1.9) | 1.9 (1.9) |
Wilson B-factor (Å2) | 12.1 | 11.1 |
Refinement | ||
Reflections used in refinement | 64,935 (496) | 47,967 (4721) |
Reflections used for Rfree | 2003 (15) | 1745 (172) |
Rwork | 0.112 (0.276) | 0.152 (0.324) |
Rfree | 0.140 (0.270) | 0.190 (0.368) |
CCwork | 0.980 (0.827) | 0.973 (0.764) |
CCfree | 0.975 (0.698) | 0.953 (0.765) |
Number of non-hydrogen atoms | 2160 | 2042 |
Protein | 1714 | 1777 |
Ligand/ion | 163 | 39 |
Water | 373 | 226 |
Protein residues | 204 | 218 |
Average B-factor (Å2) | 19.9 | 17.6 |
Protein | 14.5 | 16.0 |
Ligand/ion | 50.4 | 26.6 |
Water | 38.4 | 28.6 |
R.m.s. deviations | ||
Bond lengths (Å) | 0.007 | 0.021 |
Bond angles (°) | 1.14 | 1.84 |
Clash score | 7.38 | 7.01 |
Ramachandran plot | ||
Favoured (%) | 98.51 | 98.15 |
Allowed (%) | 1.49 | 1.85 |
Disallowed (%) | 0.00 | 0.00 |
Rotamer outliers (%) | 1.06 | 2.01 |
