TABLE 2.
Crystallographic properties, x-ray diffraction data, phasing, and refinement statistics for KshA
| KshA (Fe/S SAD)a | KshA | |
|---|---|---|
| Diffraction data | ||
| X-ray source | Cu-Kα | Canadian Light |
| Source CMCF1 | ||
| Wavelength (Å) | 1.542 | 1.000 |
| Space group | P321 | P321 |
| Unit cell (Å) | a = b = 116.1, c = 80.8 | a = b = 116.2, c = 81.0 |
| Resolution range (Å) | 61-2.5 | 50-2.3 |
| Highest shell (Å) | 2.5-2.6 | 2.3-2.36 |
| Total observations | 86,930 (1,820) | 204,950 (14,713) |
| Unique reflections | 19,620 (827) | 53,315 (3,841) |
| I/σI | 4.4 (2.2) | 14.6 (3.1) |
| Rsym (%)b | 7.0 (39.1) | 8.1 (43.5) |
| Completeness (%) | 98.6 (97.4) | 98.0 (95.1) |
| Phasing | ||
| Resolution range (Å) | 20-2.6 | |
| No. of used sites | 3 Fe–6 S | |
| Figure of merit | 0.26 | |
| Figure of merit after density modification | 0.62 | |
| Refined model | ||
| Resolution range (Å) | 20-2.3 | |
| No. of reflections | 26,909 | |
| Rfactor/Rfree (%)c | 19/23 | |
| No. of atoms | ||
| Total | 3100 | |
| Protein | 2916 | |
| Solvent | 176 | |
| Mean B values (Å2) | ||
| Protein | 42.2 | |
| Nonheme iron | 36.2 | |
| [2Fe-2S] | 32.1 | |
| rmsd | ||
| Bond lengths (Å) | 0.021 | |
| Bond angles (degrees) | 2.42 |
a
Iron/sulfur single wavelength anomalous diffraction.
b
Rsym = ΣhΣi I(hkl) – 〈I(hkl)〉/ΣhΣiI(hkl).
c
Rwork = Σ∥Fo| – |Fc∥/Σ|Fo|. Rfree is the Rwork value for 5% of the reflections excluded from the refinement. Data for the highest resolution shell are given in parentheses.