4G2P
Crystal structure of peptidyl-prolyl cis-trans isomerase domain II of molecular chaperone SurA from Salmonella enterica subsp. enterica serovar Typhimurium str. 14028S
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 | 2011-04-11 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.97921 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 43.499, 39.611, 68.581 |
| Unit cell angles | 90.00, 101.70, 90.00 |
Refinement procedure
| Resolution | 50.000 - 1.820 |
| R-factor | 0.1652 |
| Rwork | 0.161 |
| R-free | 0.23810 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1m5y |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.433 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | HKL-3000 |
| Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.850 |
| High resolution limit [Å] | 1.820 | 1.820 |
| Rmerge | 0.084 | 0.389 |
| Number of reflections | 20486 | |
| <I/σ(I)> | 34.3 | 3.7 |
| Completeness [%] | 98.8 | 90.6 |
| Redundancy | 4.4 | 3.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 297 | 0.2M Lithium sulfate, 0.1M Bis-Tris, 25% PEG3350, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 297K |
