Extended Data Table 2.
Data collection and refinement statistics for LNX2PDZ2 for EF-X experiment
| LNX2PDZ2 (OFF) | LNX2PDZ2 (200 ns) | Extrapolated Differences (8×) | |
|---|---|---|---|
| Data collection† | |||
| Space group | C2† | P1 | P1 |
| Cell dimensions | |||
| a, b, c (Å) | 65.30, 39.45, 39.01 | 38.15, 38.15, 39.01 | 38.15, 38.15, 39.01 |
| α,β,γ (°) | 90, 117.54, 90 | 113.31, 113.31,62.28 | 113.31, 113.31, 62.28 |
| Resolution (Å) | 30.08–1.80 (2.0–1.8)* | 30.08–1.80 (2.0–1.8) | 30.08–1.80 (1.86–1.80) |
| Rsym or Rmerge | 0.088 (0.051) | 0.087 (0.053) | n/a |
| I/σI | 20.7 (37.1) | 20.4 (39.9) | 6.98 (0.67) |
| Completeness (%)‡ | 75.1 (42.5) | 72.4 (38.1) | 70.2(17.8) |
| Redundancy | 5.8 (3.9) | 5.7 (3.6) | n/a |
| Refinement | |||
| Resolution (Å) | 30–1.8 (1.88–1.8) | 30–1.8 | 30–1.8 (1.88–1.8)§ |
| No. reflections¶ | 6,565 (288) | 11,568 | 11,291 (288) |
| Rwork/Rfree (%)|| | 13.2/14.8 | 28.9/31.3 | |
| No. atoms (excl. H) | 929 | 1,883 | |
| Protein | 829 | 1,712 | |
| Ligand/ion | 0 | 6 | |
| Water | 94 | 165 | |
| B-factors | 21.9 | 16.7 | |
| Protein | 19.3 | 16.0 | |
| Ligand/ion | n/a | 49.5 | |
| Water | 35.6 | 22.5 | |
| R.m.s deviations | |||
| Bond lengths (Å) | 0.020 | 0.018 | |
| Bond angles (°) | 1.63 | 1.80 | |
All data were collected from a single crystal of LNX2PDZ2 using Laue crystallography.
Highest-resolution shell is shown in parentheses. Data reduction in Precognition (Renz Research) differs from conventional data reduction in that weak spots are discarded a priori, resulting in low apparent completeness and high apparent signal and Rmerge, especially at high resolution. Note also that data statistics are reported after global scaling. Subsequent local scaling slightly affects statistics but this scaling mode does not report full last shell statistics. Extrapolated differences were assessed in Xtriage (PHENIX).
For the purpose of refinement of the OFF model, P1 reflections were merged according to C2 symmetry (merging R factor for this: 0.077).
See Supplementary Table 3 for data collection and reduction statistics as reported traditionally for Laue crystallography, including assessment of completeness in both C2 and P1. Reported data collection statistics refer to P1.
Data were retained to the resolution of the two ‘parent’ data sets (OFF and 200 ns); effective resolution based on propagation of errors is 2.3 Å; completeness over 30–2.3 Å is 89.9%.
Test sets comprised 5% and 10% of reflections for refinement of the OFF model and refinement against extrapolated structure factors, respectively.
The matching number of reflections in the high-resolution shell is coincidental.