4AY4
crystal structure of Bacillus anthracis PurE
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-2 |
| Synchrotron site | ESRF |
| Beamline | ID14-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-12-12 |
| Detector | ADSC CCD |
| Spacegroup name | P 65 2 2 |
| Unit cell lengths | 87.003, 87.003, 270.002 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 43.930 - 2.000 |
| R-factor | 0.14893 |
| Rwork | 0.147 |
| R-free | 0.17988 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1xmp |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.404 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.7.0029) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.070 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.070 | 0.290 |
| Number of reflections | 42925 | |
| <I/σ(I)> | 32.66 | 5.82 |
| Completeness [%] | 96.6 | 94.1 |
| Redundancy | 8.1 | 6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 8.5 | PROTEIN WAS CRYSTALLIZED FROM 0.1M TRIS PH8.5, 0.3M SODIUM ACETATE, 15% PEG 4K |
