3RMS
Crystal structure of uncharacterized protein Svir_20580 from Saccharomonospora viridis
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-BM |
| Synchrotron site | APS |
| Beamline | 19-BM |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-10-03 |
| Detector | ADSC QUANTUM 210r |
| Wavelength(s) | 0.97931 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 44.630, 60.968, 73.209 |
| Unit cell angles | 90.00, 96.77, 90.00 |
Refinement procedure
| Resolution | 33.441 - 2.133 |
| R-factor | 0.1781 |
| Rwork | 0.177 |
| R-free | 0.20460 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3rmq |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.268 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | PHASER |
| Refinement software | PHENIX ((phenix.refine: dev_610)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.190 |
| High resolution limit [Å] | 2.130 | 2.130 |
| Rmerge | 0.081 | 0.641 |
| Number of reflections | 21709 | |
| <I/σ(I)> | 17.6 | 2 |
| Completeness [%] | 99.8 | 99.9 |
| Redundancy | 3.3 | 3.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 297 | 0.2 M proline, 0.1 M HEPES, 10% PEG3350, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 297K |
