Table 1.
Data collection, phasing and refinement statistics for MAD (SeMet)
| Native1 | SeMet1 | |||
|---|---|---|---|---|
| Data collection | ||||
| Space group | P6122 | |||
| Cell dimensions | ||||
| a, b, c (Å) | 70.8, 70.8, 512.4 | 71.2, 71.2, 513.4 | ||
| α, β, γ (°) | 90, 90, 120 | 90, 90, 120 | ||
| Peak (E1) | Inflection (E2) | Remote (E3) | ||
| Wavelength (Å) | 1.0332 | 0.9794 | 0.9796 | 0.9494 |
| Resolution (Å) | 19.8–2.4 (2.53-2.4) | 2.8 (2.9-2.8) | 2.8 (2.9-2.8) | 2.8 (3.0-2.8) |
| Rmerge | 0.084 | 0.081 | 0.082 | 0.083 |
| Mn(I/sd) | 19.4 (1.9) | 16.5 (4.5) | 16.4 (4.3) | 17.3 (3.9) |
| Total reflection | 485,811 | 220,658 | 220,938 | 242,804 |
| Unique reflection | 31,135 | 20,321 | 20,304 | 20,353 |
| Completeness (%) | 99.2 (99.3) | 99.5 (99.8) | 99.5 (99.8) | 99.6 (99.8) |
| Redundancy | 15.4 (15.9) | 9.2 (9.5) | 9.1 (9.5) | 9.1 (9.5) |
| Refinement | ||||
| Resolution (Å) | 18.8–2.4 | |||
| Rwork (%) / Rfree2(%) | 20.0/22.9 | |||
| No. atoms | 3,959 | |||
| Protein | 3,937 | |||
| Water | 22 | |||
| B-factors | ||||
| Protein | 95.7 | |||
| Water | 93.5 | |||
| Rmsd | ||||
| Bond lengths (Å) | 0.010 | |||
| Bond angles (°) | 1.12 | |||
| Ramachandran plot | ||||
| Favored (%) | 99.37% | |||
| Outliers (%) | 0.0% | |||
Two crystals were used for data collection, one native and one SeMet.
1
Values in parentheses are for highest-resolution shell as defined in the resolution row.
2
Rfree is defined as 5% of initial total number of reflections. Rmsd bond lengths and angles are the deviations from ideal values.
3
Mn(I/sd) is defined as <merged<Ih>/sd(<Ih>) > ~= signal/noise