3UMA
Crystal structure of a hypothetical peroxiredoxin protein frm Sinorhizobium meliloti
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X25 |
| Synchrotron site | NSLS |
| Beamline | X25 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2011-11-06 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.9795 |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 113.063, 113.063, 98.823 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 48.960 - 2.200 |
| R-factor | 0.21428 |
| Rwork | 0.213 |
| R-free | 0.24060 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2wfc |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.223 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0110) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.280 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.083 | 0.388 |
| Number of reflections | 37257 | |
| <I/σ(I)> | 7.6 | |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 19.9 | 19.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 293 | 2.0M Ammonium Sulfate, 0.1M HEPES, PEG 400, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
