TABLE 1.
Data collection and refinement statistics
| Data collecteda | Value(s) |
|---|---|
| Resolution (Å) | 50.0-3.5 (3.63-3.50) |
| Rmerge | 0.223 (0.783) |
| I/σI | 13.25 (1.64) |
| % Completeness | 98.7 (92.0) |
| Redundancy | 12.1 (7.1) |
| Refinement | |
| Resolution (Å) | 25-3.5 |
| No. of reflections (working set) | 6,475 |
| No. of reflections (test set) | 311 |
| Rwork, Rfree | 0.2084, 0.2967 |
| No. of protein atoms | 2,905 |
| Avg B factors (residual after TLS refinementb) | |
| Protein (Å2) | 63 |
| Chloride ion, water (Å2) | 19 |
| RMS deviations (geometry) | |
| Bond length (Å) | 0.0179 |
| Bond angle (°) | 1.69 |
Rmerge, Σh,k,lΣi|Ii(hkl) − 〈I(hkl)〉|/Σh,k,lΣiIi(hkl), where I is an intensity that is observed i times; I/σI, signal-to-noise ratio (average observed intensity divided by average standard deviation of the observed intensity); Rwork, Σh,k,l||Fobs| − |Fcalc||/Σh,k,l|Fobs|, where h, k, l cover the “working set” of observed structure factor amplitude (Fobs) reflections used in refinement (all reflections minus the test set) and Fcalc is the calculated structure factor amplitude; Rfree, Σh,k,l||Fobs| − |Fcalc||/Σh,k,l|Fobs|, where h, k, l cover the “test set,” 5% of randomly selected Fobs reflections sequestered before refinement and not used in refinement; RMS, root mean square. Values for the highest-resolution shell (3.63 to 3.50 Å) are shown in parentheses.
See the Protein Data Bank entry for TLS tensor refinement parameters.