4EW5
C-terminal domain of inner membrane protein CigR from Salmonella enterica.
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 | 2011-10-19 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9792 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 49.870, 54.811, 73.992 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 41.400 - 1.870 |
| R-factor | 0.1783 |
| Rwork | 0.176 |
| R-free | 0.23010 |
| Structure solution method | SAD |
| RMSD bond length | 0.019 |
| RMSD bond angle | 1.830 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | SHELXD |
| Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 41.400 | 50.000 | 1.910 |
| High resolution limit [Å] | 1.870 | 5.100 | 1.880 |
| Rmerge | 0.107 | 0.072 | 0.811 |
| Number of reflections | 17270 | ||
| <I/σ(I)> | 8.9 | 2.2 | |
| Completeness [%] | 99.9 | 99.1 | 100 |
| Redundancy | 6.8 | 6.3 | 5.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 289 | 0.1M Hepes buffer, 2% PEG-400, 2M Ammonium sulphate. Full length protein was crystallized in presence of V8 protease., pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 289K |






