TABLE 1.
Crystallographic data and refinement summary
Values for highest resolution shell are shown in parentheses. Five percent of the reflections were set aside for calculation of the Rfree. Crystallographic and refinement statistics were calculated by Scala (26) and Refmac5 (31), respectively.
| RraA + SrmB | RraA + RhlB(398–421) | |
|---|---|---|
| Crystallization condition | 100 mm MOPS pH 7.2 | 100 mm Sodium citrate pH 5.4 |
| 12% PEG 8000 | MPD 32% (v/v) | |
| 100 mm Magnesium acetate | 200 mm Ammonium acetate | |
| Space group | P3221 | C2 |
| Cryo-protectant | 25% glycerol (v/v) | |
| Wavelength (Å) | 0.9763 | 0.9795 |
| Resolution (Å) | 63.56–2.90 (3.06–2.90) | 63.53–2.80 (2.95–2.80) |
| Unit cell dimensions | ||
| a, b, c (Å) | 73.39, 73.39, 222.89 | 259.63, 69.07, 123.30 |
| α, β, γ (°) | 90.00, 90.00, 120.00 | 90.00, 109.17, 90.00 |
| Completeness (%) | 99.6 (99.5) | 98.0 (99.3) |
| Multiplicity | 4.0 (4.1) | 2.9 (2.9) |
| I/σ | 10.2 (2.8) | 15.5 (3.7) |
| Rmerge (%) | 12.3 (50.8) | 4.9 (25.9) |
| Refinement | ||
| Reflections | 15,208 | 47,500 |
| R factor | 0.2012 | 0.2303 |
| Rfree | 0.2509 | 0.2900 |
| Bond lengths root mean square deviations (Å) | 0.0228 | 0.0168 |
| B factor protein (Å2) | 42 | 46 |
| Atoms | 4,993 | 14,445 |
| Residues | 673 | 1970 |