Table 1.
Summary of single isomorphous replacement phase determination and refinement statistics
| Crystal
|
||||
|---|---|---|---|---|
| Native | MeHgNO3 | MeHgNO3 | MeHgNO3 | |
| Data collection | ||||
| Max. resolution (Å) | 2.3 | 2.7 | 2.8 | 3.1 |
| Completeness (%) | 97 | 58 | 80 | 91 |
| Rsym (%) | 6.3 | 5.9 | 5.3 | 7.7 |
| Rder (%) | 34 | 32 | 33 | |
| Phasing power (Acen/Cen) | 2.22/1.56 | 2.14/1.59 | 2.11/1.50 | |
| Number of sites | 2 | 2 | 2 | |
| Reflections, observed | 91,581 | 19,398 | 26,511 | 25,198 |
| Reflections, unique | 29,443 | 10.489 | 13,339 | 11,085 |
| Refinement statistics | ||||
| Refinement resolution | 8.0–2.3 Å | |||
| Reflections used | 26,412 | |||
| Completeness of working set (1σ/2σ) | 82%/57% | |||
| Rwork factors (1σ/2σ) | 22.4/19.1 | |||
| Rtest factors (1σ/2σ) | 27.5/24.7 | |||
| rms deviation bond lengths/bond angles | 0.008 Å/1.38° | |||
| B-value (average/bonded SD) | 3.61 Å/2.06 Å2 | |||
Space group, P65. Unit cell, a = b = 120.44, c = 79.60. Rsym = ∑ |I-〈I〉|/∑I, where I is the observed intensity and 〈I〉 is the average intensity of multiple observations of symmetry related reflections. Rder = ∑ ∥ FPH|− |FP∥/∑|Fp|, where |FP| is the protein structure factor amplitude and |FPH| is the heavy atom structure factor amplitude. Phasing power = rms (|FH|/E), where |FH| is the heavy atom structure factor amplitude and E is the residual lack of closure error. Figure of merit = 〈∑P(α)eiα/∑P(α)〉, in which α is the phase and P(α) is the phase probability distribution. R = ∑∥Fo|−|Fc∥/∑|Fo|, where Rtest is calculated for a randomly chosen 5% of reflections, Rwork is calculated for the remaining 95% of reflections used for structure refinement.