5EV7
The crystal structure of a functionally unknown conserved protein mutant from Bacillus anthracis str. Ames
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 | 2015-06-05 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.97929 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 73.157, 155.567, 49.152 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 36.578 - 2.351 |
| R-factor | 0.2194 |
| Rwork | 0.218 |
| R-free | 0.25100 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4fca |
| RMSD bond length | 0.002 |
| RMSD bond angle | 0.619 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | HKL-3000 |
| Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 37.000 | 2.390 |
| High resolution limit [Å] | 2.350 | 2.350 |
| Rmerge | 0.109 | 0.795 |
| Number of reflections | 24158 | |
| <I/σ(I)> | 23.4 | 2.9 |
| Completeness [%] | 99.9 | 100 |
| Redundancy | 6.2 | 5.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 289 | 24% (w/v) PEG1500, 20% (v/v) glycerol |
