Table 1.
Summary of Crystal and SAD Data Collection
unit cell parameters |
a = 40.50 Å, b = 73.88 Å, c = 92.25 Å, α = β = γ = 90° |
space group | P212121 |
molecular massa (Da) | 33810 |
no. of molecules per asymmetric unit | 1 |
no. of selenomethionine residues per asymmetric unit |
1 |
wavelength (Å) | 0.9791 |
resolution limit (Å) | 1.70 |
no. of unique reflections | 31255 |
overall data completeness (%) | 99.4 |
overall data redundancy | 10.45 |
overall Rmerge (%) | 6.9 |
figure of merit (FOM) | 0.2967 |
phasing power | 1.6309 |
Refinement Statistics | |
resolution range (Å) | 50.0–1.7 (1.81–1.7)b |
no. of reflections (unique) | 58916 (9343)b |
no. of reflections (observed) | 55440 (7699)b |
percent reflections observed | 94.1 (82.4)b |
σ cutoff | 0.0 |
overall R factor (%) | 20.0 (30.5)b |
Rfree (%) | 23.6 (31.6)b |
rms deviations from ideal geometry | |
bond lengths (Å) | 0.006 |
angles (deg) | 1.3 |
dihedrals (deg) | 22.6 |
impropers (deg) | 0.81 |
no. of protein non-hydrogen atoms | 1977 |
no. of water molecules | 292 |
mean B factor (Å2) | 26.5 |
Ramachandran plot statistics (%) | |
residues in most favored regions | 98.3 |
residues in additional allowed regions | 1.7 |
residues in disallowed regions | 0.0 |
Molecular mass of the polypeptide with 33-residue tag fused to residues 19–280 of GmpC.
Values in parentheses are for the highest-resolution shell.