5F2V
Crystal structure of the small alarmone synthethase 1 from Bacillus subtilis bound to AMPCPP
Replaces: 5DEEExperimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-1 |
| Synchrotron site | ESRF |
| Beamline | ID23-1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2014-03-06 |
| Detector | PSI PILATUS 6M |
| Wavelength(s) | 0.97934 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 116.671, 103.631, 138.290 |
| Unit cell angles | 90.00, 104.84, 90.00 |
Refinement procedure
| Resolution | 48.310 - 2.800 |
| R-factor | 0.1943 |
| Rwork | 0.193 |
| R-free | 0.26370 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5dec |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.172 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.9_1685) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 48.310 | 2.950 |
| High resolution limit [Å] | 2.800 | 2.800 |
| Rmerge | 0.090 | 0.486 |
| Number of reflections | 78602 | |
| <I/σ(I)> | 2.8 | 2.8 |
| Completeness [%] | 1.0 | 0.895 |
| Redundancy | 3.8 | 3.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 293 | 0.2 M KSCN, 20% (W/V) PEG3350 |
