Table 1.
Crystallographic Data and Refinement Statistics
| A. Data Collectiona | ||||||
|---|---|---|---|---|---|---|
| Wavelength (Å) | Resolution (Å) | % Complete | Rsymb | % I/σ > 3 | Redundancy | |
| MAD Phasing | 0.9795 (peak) | 25 – 3.25 | 93.8 (97.1) | 0.074 (0.323) | 72.4 (36.2) | 1.9 (1.9) |
| 0.9797 (edge) | 25 – 3.25 | 94.2 (96.9) | 0.072 (0.319) | 73.1 (37.7) | 1.9 (1.9) | |
| 0.9643 (remote) | 25 – 3.25 | 94.2 (97.1) | 0.073 (0.315) | 73.1 (38.5) | 1.9 (1.9) | |
| B. Refinement | ||||||
|---|---|---|---|---|---|---|
| Data | Wavelength (Å) | Resolution (Å) | % Complete | Rsym | % I/σ > 3 | Redundancy |
| 1.000 | 25-3.0 (3.11-3.00) | 94.4 (96.1) | 0.057 (0.351) | 80.3 (46.5) | 6.8 (6.7) | |
| Model | Rcrystc | Rfree | Protein atoms | Average B | Rmsd bonds (Å) | Rmsd Angles (°) |
| 0.256 | 0.292 | 2606 | 69 | 0.009 | 1.56 | |
a
Values in parentheses are for the highest resolution shell: 2.59-2.50 Å for the MAD phasing data sets.
b
Rsym=ΣhΣi |(Ii(h)-< I(h)>|/ ΣhΣi Ii(h), where Ii(h) is the I-th measurement of reflection h, and <I(h)> is the weighted mean of all measurements of h. Bijvoet measurements were treated as independent reflections for the MAD phasing data sets.
c
Rcryst = Σ|Fobs-Fcalc|/ΣFobs where Fobs = observed structure factor amplitude and Fcalc = structure factor calculated from model. Rfree is computed in the same manner as Rcryst, using the test set of reflections.