3FRW
Crystal structure of putative TrpR protein from Ruminococcus obeum
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-12-12 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.9792 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 67.601, 110.991, 77.262 |
| Unit cell angles | 90.00, 101.47, 90.00 |
Refinement procedure
| Resolution | 42.300 - 2.050 |
| R-factor | 0.182 |
| Rwork | 0.180 |
| R-free | 0.21800 |
| Structure solution method | SAD |
| RMSD bond length | 0.018 |
| RMSD bond angle | 1.486 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | SHELXD |
| Refinement software | REFMAC (5.5.0054) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 42.300 | 2.090 |
| High resolution limit [Å] | 2.050 | 2.050 |
| Rmerge | 0.105 | 0.803 |
| Number of reflections | 69539 | |
| <I/σ(I)> | 34.781 | 3.37 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 7.5 | 7.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.4 | 289 | 0.2 M Sodium acetate, 20% PEG 3350, pH 7.4, VAPOR DIFFUSION, SITTING DROP, temperature 289K |
