TABLE II.
Phasing | ||||||
---|---|---|---|---|---|---|
Resolution range | Inf | Peak | h-Remote | All | ||
39–2.4 Å | Fried | Iso | Fried | Iso | Fried | |
Phasing power | 3.05 | 1.91 | 2.71 | 1.33 | 1.74 | |
FOM | 0.45 | 0.38 | 0.43 | 0.30 | 0.32 | 0.75 |
Density modification, FOM (1.8 Å) | 0.96 | |||||
Refinement | ||||||
Resolution range (Å) | 39–1.63 | |||||
No. of reflections | 35198 | |||||
σ cutoff | 0 | |||||
R-value | 0.194 | |||||
Free R-value | 0.214 (4024) | |||||
RMSD from ideal geometry | ||||||
Bond length (1–2) (Å) | 0.005 | |||||
Angle (°) | 1.20 | |||||
Dihedral (°) | 21.9 | |||||
Improper (°) | 0.84 | |||||
Mean B-factor (Å2) | ||||||
All atoms | 18.70 | |||||
Protein atoms (2149) | ||||||
Protein main chain | 16.95 | |||||
Protein side chain | 15.70 | |||||
Formate (3) | 12.52 | |||||
Mg (2) | 8.69 | |||||
Glycerol (12) | 29.26 | |||||
Water (272) | 30.76 | |||||
Ramachandran plot statistics (%) | ||||||
Residues in most favored regions | 100 | |||||
Residues in additional allowed regions | 0.0 | |||||
Residues in disallowed region | 0.0 |