5F4B
Structure of B. abortus WrbA-related protein A (WrpA)
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 | 2014-11-24 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.97924 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 63.580, 63.580, 188.537 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 44.696 - 2.498 |
| R-factor | 0.2314 |
| Rwork | 0.230 |
| R-free | 0.26900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | The 2.4 A structure of Apo-protein solved by SAD phasing |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.618 |
| 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] | 44.700 | 2.540 |
| High resolution limit [Å] | 2.498 | 2.498 |
| Rmerge | 0.777 | |
| Number of reflections | 14207 | |
| <I/σ(I)> | 11.26 | 1.82 |
| Completeness [%] | 99.7 | 100 |
| Redundancy | 5.3 | 5.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.3 | 289 | 0.2 M potassium formate pH 7.3, 20 % (w/v) PEG 3350 |
