4QMK
Crystal structure of type III effector protein ExoU (exoU)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-G |
| Synchrotron site | APS |
| Beamline | 21-ID-G |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2013-10-14 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.97856 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 67.218, 115.341, 88.443 |
| Unit cell angles | 90.00, 102.77, 90.00 |
Refinement procedure
| Resolution | 29.860 - 2.500 |
| R-factor | 0.20912 |
| Rwork | 0.206 |
| R-free | 0.26978 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3tu3 |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.609 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.7.0029) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.540 |
| High resolution limit [Å] | 2.500 | 2.500 |
| Rmerge | 0.070 | 0.441 |
| Number of reflections | 43226 | |
| <I/σ(I)> | 15.7 | 2.05 |
| Completeness [%] | 95.2 | 75.7 |
| Redundancy | 3.7 | 2.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 295 | protein: 5.8 mg/ml in 10 mM Tris-HCl pH 8.3, 500 mM NaCl, 5 mM BME. Crystallization conditions: The Classics II Suite (#G7:79): 0.2 M Ammonium acetate, 0.1 M Bis-Tris (pH 6.5), 25% (w/v) PEG 3350, VAPOR DIFFUSION, SITTING DROP, temperature 295K |
