Table 1. Summary of crystallographic analysis for MerR.
| Protein | Se_MerR | apo-MerR | Se_Hg2+-MerR | Hg2+-MerR | ||
|---|---|---|---|---|---|---|
| Space group | P21 | P21 | P222 | P222 | ||
| Unit cell dimensions | ||||||
| a (Å) | 80.63 | 80.54 | 70.00 | 69.89 | ||
| b (Å) | 94.89 | 94.80 | 70.55 | 70.96 | ||
| c (Å) | 86.88 | 87.06 | 71.61 | 71.38 | ||
| Data collection | Se-inflection | Se-remote | Se-inflection | Se-remote | ||
| Wavelength (Å) | 0.9791 | 0.9537 | 1.0000 | 0.9792 | 0.9610 | 0.9224 |
| Resolution (Å) | 30–2.75 | 30–2.75 | 30–2.61 | 30–3.7 | 30–3.7 | 30–2.56 |
| No. of observed reflections | 140,766 | 151,989 | 137,710 | 37,272 | 37,100 | 137,888 |
| Unique reflections | 28,526 | 28,752 | 38,485 | 3.957 | 3.937 | 11,808 |
| Completeness (last shell)a (%) | 85.4(66.0) | 86.1(70.5) | 99.0(99.9) | 97.1(98.6) | 96.9(98.6) | 99.7(98.5) |
| Multiplicity | 5.3 | 5.3 | 3.6 | 9.4 | 9.4 | 11.7 |
| Rsym (last shell)a,b (%) | 8.3(40.5) | 8.7(37.5) | 8.3(40.5) | 21.8(48.9) | 23.2(50.1) | 13(52.1) |
| Refinement | ||||||
| Resolution range (Å) | 30–2.61 | 30–2.56 | ||||
| No. of reflection in working set (test set) | 36,559(1962) | 10630(1178) | ||||
| Rcryst (last shell)c | 22.5(28.5) | 22.5(22.3) | ||||
| Rfree (last shell)c | 25.7(30.7) | 28.7(34.5) | ||||
| Rmsd from ideal | ||||||
| Bond lengths (Å) | 0.003 | 0.011 | ||||
| Bond angle (deg.) | 0.67 | 1.67 | ||||
| Ramachandran outliers (%) | 0 | 0 | ||||
| Number of macromolecules | 7166 | 1943 | ||||
| Ligands | 0 | 2 | ||||
| H2O | 97 | 38 | ||||
| Average B-factor (protein/water/ligand) | 58.4(58.5/50.3/NA) | 39.5(39.6/36.9/37.7) | ||||
aStatistics for data from the resolution shell of 2.85–2.75 Å (Se_apo-MerR data), 2.68–2.61 Å (apo-MerR data), 3.99–3.7 Å (Se_Hg2+-MerR data) and 2.68–2.56 Å (Hg2+-MerR data).
bRsym = (Σ|Ihkl - <I>|)/(ΣIhkl), where the average intensity <I>is taken overall symmetry equivalent measurements and Ihkl is the measured intensity for any given refection.
cRcryst = (Σ∥Fo| - k|Fc∥)/(Σ|Fo|). Rfree = Rcryst for a randomly selected subset (5%) of the data that were not used for minimization of the crystallographic residual.