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 |