Table 2. Summary of crystallographic data for native protein and Se-MAD data.
Values in parentheses are for the highest resolution shell.
| Native | Se edge | Se inflection | Se remote | |
|---|---|---|---|---|
| Wavelength (Å) | 1.5417 | 0.9793 | 0.9794 | 0.9747 |
| Resolution (Å) | 50–3.0 (3.1–3.0) | 50–2.9 (3.0–2.9) | 50–3.0 (3.1–3.0) | 50–3.0 (3.0–2.9) |
| Unit-cell parameters (Å, °) | a = 134.60, b = 134.60, c = 192.11, β = 120 | a = 133.38, b = 133.38, c = 191.89, β = 120 | a = 133.23, b = 133.23, c = 192.28, β = 120 | a = 133.28, b = 133.28, c = 192.14, β = 120 |
| No. of measurements | 228866 | 124206 | 122564 | 114030 |
| No. of unique reflections | 18521 (844) | 18122 (695) | 16548 (335) | 17492 (617) |
| Redundancy | 12.4 (9.5) | 6.9 (4.4) | 7.4 (4.7) | 6.5 (3.9) |
| Completeness (%) | 86.6 (40.9) | 78.9 (31.2) | 79.5 (16.7) | 75.9 (27.6) |
| Rmerge† | 0.124 (0.722) | 0.072 (0.301) | 0.077 (0.386) | 0.072 (0.349) |
| 〈I/σ(I)〉 | 16.7 (1.9) | 23.8 (2.9) | 16.8 (2.3) | 23.1 (2.4) |
†
R
merge = 
, where I(h, i) is the intensity of the ith observation of reflection h and 〈I(h)〉 is the average intensity of redundant measurements of reflection h.