3DEU
Crystal structure of transcription regulatory protein slyA from Salmonella typhimurium in complex with salicylate ligands
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 23-ID-D |
| Synchrotron site | APS |
| Beamline | 23-ID-D |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-11-03 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 1.37760 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 63.382, 78.019, 84.385 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.300 |
| R-factor | 0.229 |
| Rwork | 0.228 |
| R-free | 0.25900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2fbh |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.986 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.070 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.074 | |
| Number of reflections | 27988 | |
| <I/σ(I)> | 31.7 | 1.1 |
| Completeness [%] | 96.4 | 90.8 |
| Redundancy | 12.9 | 7.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 4.2 | 298 | 20% PEG 300, 10% Glycerol, 0.1 M Phosphate/citrate buffer pH 4.2, 0.2 M Ammonium sulfate, 50 mM Sodium salicylate, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
