5ANP
CRYSTAL STRUCTURE OF THE BA41 PROTEIN FROM BIZIONIA ARGENTINENSIS
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SOLEIL BEAMLINE PROXIMA 1 |
| Synchrotron site | SOLEIL |
| Beamline | PROXIMA 1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Detector | DECTRIS PILATUS 6M |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 34.623, 58.135, 60.198 |
| Unit cell angles | 90.00, 96.04, 90.00 |
Refinement procedure
| Resolution | 34.430 - 1.400 |
| R-factor | 0.1761 |
| Rwork | 0.175 |
| R-free | 0.18890 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2kw7 |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.030 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | BUSTER (2.10.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 34.430 | 1.420 |
| High resolution limit [Å] | 1.400 | 1.400 |
| Rmerge | 0.080 | 0.790 |
| Number of reflections | 46549 | |
| <I/σ(I)> | 11.6 | 2.2 |
| Completeness [%] | 99.5 | 99.5 |
| Redundancy | 4.6 | 4.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 6.1 | 23% PEG 5000 MME, 2% PEG 400, 0.1M IMIDAZOLE PH 6.1 |
