4OA3
Crystal structure of the BA42 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 |
| Collection date | 2013-11-26 |
| Detector | PSI PILATUS 6M |
| Wavelength(s) | 0.97857 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 31.920, 39.620, 106.970 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.590 - 1.390 |
| R-factor | 0.176 |
| Rwork | 0.174 |
| R-free | 0.20480 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2lt2 |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.050 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | AMoRE |
| Refinement software | BUSTER (2.10.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.470 |
| High resolution limit [Å] | 1.390 | 1.390 |
| Rmerge | 0.049 | 0.695 |
| Number of reflections | 27591 | |
| <I/σ(I)> | 16.01 | 1.99 |
| Completeness [%] | 98.1 | 96.8 |
| Redundancy | 4.31 | 4.35 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 294 | 24% PEG 2000 MME, 0.1M MES pH 6.5, 0.1M sodium acetate, VAPOR DIFFUSION, HANGING DROP, temperature 294K |
