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 |
a
Molecular mass of the polypeptide with 33-residue tag fused to residues 19–280 of GmpC.
b
Values in parentheses are for the highest-resolution shell.