3QRA
The crystal structure of Ail, the attachment invasion locus protein of Yersinia pestis
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-10-20 |
| Detector | MARMOSAIC 300 mm CCD |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 50.236, 50.236, 170.623 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 34.777 - 1.801 |
| R-factor | 0.1999 |
| Rwork | 0.199 |
| R-free | 0.22840 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1qj8 |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.259 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX ((phenix.refine: dev_572)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 37.700 | 1.860 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Number of reflections | 19652 | |
| <I/σ(I)> | 44.1 | 3.9 |
| Completeness [%] | 93.0 | 68 |
| Redundancy | 12.3 | 4.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 298 | 34% PEG1000, 0.2 M potassium fluoride, 0.1 M Bis-Tris, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
