TABLE 2.
Statistic type | Native | Selenomethionine derivative |
||
---|---|---|---|---|
Peak | Remote | Inflection | ||
Data collection | ||||
Wavelength (Å) | 1.0 | 0.9793 | 0.913 | 0.9797 |
Space group | P1 | P1 | P1 | P1 |
Cell dimensions | ||||
a, b, c | 31.56, 37.53, 63.91 | 31.70, 38.13, 64.08 | 31.73, 38.22, 64.13 | 31.71, 38.17, 64.19 |
Alpha, beta, gamma | 85.45, 82.26, 81.26 | 85.60, 82.06, 81.54 | 85.64, 82.10, 81.28 | 85.56, 82.06, 81.45 |
Resolution range (Å) | 37.03–1.7 (1.79–1.7)a | 37.65–1.86 (1.96–1.86) | 37.72–1.73 (1.82–1.73) | 37.68–1.86 (1.96–1.86) |
No. of total reflections | 113,354 (15,961) | 92,762 (13,115) | 114,487 (16,212) | 93,035 (13,094) |
No. of unique reflections | 29,564 (4,221) | 23,720 (3,384) | 29,331 (4,195) | 23,733 (3,384) |
Rsym (%) | 0.074 (0.424) | 0.081 (0.617) | 0.092 (0.858) | 0.070 (0.645) |
Mean I/sigma(I) | 10.8 (2.8) | 9.4 (1.7) | 7.6 (0.8) | 10.8 (1.6) |
Multiplicity | 3.8 (3.8) | 3.9 (3.9) | 3.9 (3.9) | 3.9 (3.9) |
Completeness (%) | 93.7 (91.7) | 95.6 (93.5) | 95.4 (93.3) | 95.3 (93.1) |
Refinement | ||||
Resolution (Å) | 31.6/1.7 | |||
R-factor | 0.19 (0.27) | |||
R-free | 0.21 (0.32) | |||
No. of atoms | 2,589 | |||
Macromolecules | ||||
Protein | 2,168 | |||
Ligand/ion | 2 | |||
Water | 419 | |||
Protein residues | 262 | |||
B-factors | 29.7 | |||
Protein | 28.1 | |||
Solvent | 37.8 | |||
RMSD | ||||
Bond lengths (Å) | 0.006 | |||
Bond angles (°) | 0.879 | |||
Ramachandran favored (%) | 98.6 | |||
Ramachandran outliers (%) | 0.39 | |||
Clash score | 5.57 |
Values in parentheses are stated for the highest-resolution bin for each structure.
Data collection statistics are shown for the native data set and those used for MAD phasing (peak, inflection, and remote). The final model was refined against the native set.