1H4Z
Structure of the Anti-Sigma Factor Antagonist SpoIIAA in its Unphosphorylated Form
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-3 |
| Synchrotron site | ESRF |
| Beamline | ID14-3 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Spacegroup name | P 65 2 2 |
| Unit cell lengths | 81.582, 81.582, 71.616 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 20.000 - 2.740 |
| R-factor | 0.25 * |
| Rwork | 0.251 |
| R-free | 0.30500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1h4x |
| RMSD bond length | 0.020 * |
| RMSD bond angle | 2.021 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.840 |
| High resolution limit [Å] | 2.740 | 2.740 |
| Rmerge | 0.072 | 0.342 |
| Total number of observations | 26991 * | |
| Number of reflections | 4022 | |
| <I/σ(I)> | 23.5 | 5.3 |
| Completeness [%] | 99.8 | 99.7 |
| Redundancy | 6.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 8.5 * | 291 * | Seavers, P.R., (2001) Acta Crystallogr., D57, 292. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 5 (mg/ml) | |
| 2 | 1 | drop | Tris-HCl | 10 (mM) | |
| 3 | 1 | drop | 50 (mM) | ||
| 4 | 1 | drop | dithiothreitol | 1 (mM) | |
| 5 | 1 | reservoir | PEG4000 | 15 (%) | |
| 6 | 1 | reservoir | 200 (mM) | ||
| 7 | 1 | reservoir | Tris-HCl | 100 (mM) |
