5J44
Crystal structure of the Secreted Extracellular protein A (SepA) from Shigella flexneri
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 31-ID |
| Synchrotron site | APS |
| Beamline | 31-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2014-12-01 |
| Detector | RAYONIX MX225HE |
| Wavelength(s) | 0.97931 |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 143.520, 143.520, 269.250 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 72.763 - 2.912 |
| R-factor | 0.2156 |
| Rwork | 0.214 |
| R-free | 0.23880 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1wxr |
| RMSD bond length | 0.001 |
| RMSD bond angle | 0.469 |
| Data reduction software | iMOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.10_2155: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 72.763 | 3.000 |
| High resolution limit [Å] | 2.912 | 2.912 |
| Rmerge | 0.320 | 1.700 |
| Number of reflections | 70949 | |
| <I/σ(I)> | 7.73 | 1.4 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 10.4 | 8.8 |
| CC(1/2) | 1.000 | 0.300 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 298 | A 1:1 ratio of 10mg/ml protein was mixed with the following - 0.085M MES/IMID pH 6.5, 0.015M Na HEPES pH 7.5, 8.5% PEG 8K, 17% ethylene glycol, 0.03M MgCl2 and 4.5% PEG 400 |
