Table 1. Data collection, phasing, and refinement statistics for human NEIL1.
| Native | SeMet | SeMet-I | I | |
|---|---|---|---|---|
| Data collection statistics | ||||
| Resolution, Å | 30-2.10 | 20-2.30 | 20-2.40 | 20-2.30 |
| Unique reflections | 19,225 | 14,770 | 12,854 | 14,357 |
| Redundancy | 12 | 5 | 6 | 3 |
| Rmerge* | 0.085 (0.383) | 0.095 (0.437) | 0.089 (0.292) | 0.078 (0.241) |
| Completeness,* % | 95.1 (100) | 99.9 (100) | 98.4 (91) | 97.0 (85.5) |
| Overall I/σ〈I〉* | 39.6 (5.6) | 13.7 (2.8) | 19.5 (2.8) | 15.8 (2.5) |
| MIR phasing statistics | ||||
| No. of sites | 4 Se | 4 Se, 5 I | 8 I | |
| Phasing power | 0.39 | 0.74 | 1.0 | |
| Figure of merit (solve) | 0.543 | |||
| Figure of merit (resolve) | 0.717 | |||
| Refinement statistics | ||||
| Rwork, % | 19.4 | |||
| Rfree, % | 23.1 | |||
| rms deviations | ||||
| Bond length, Å | 0.0053 | |||
| Bond angles, ° | 1.29 | |||
| B-factor, Å2 | ||||
| Protein | 28 | |||
| Water | 37 |
Rmerge = Σ |I - 〈I〉|/ Σ I, where 〈I〉 is the average intensity from multiple observations of symmetry-related reflections. Phasing power = ΣhklFH/Σ|FPH - FPH,calc|. Rwork and Rfree = Σ ||Fo| - |Fc||/Σ |Fo|, where Fo and Fc are the observed and calculated structure factor amplitudes, respectively. Rfree was calculated with ≈10% of the reflections not used in refinement. MIR, multiple isomorphous replacement; I, iodide; Se, selenium.
*
Values for the highest resolution shell are shown in parentheses.