3ZTT
Crystal structure of pneumococcal surface antigen PsaA with manganese
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX2 |
| Synchrotron site | Australian Synchrotron |
| Beamline | MX2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Detector | ADSC QUANTUM 315 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 68.334, 107.693, 77.942 |
| Unit cell angles | 90.00, 95.67, 90.00 |
Refinement procedure
| Resolution | 19.730 - 2.700 |
| R-factor | 0.21668 |
| Rwork | 0.215 |
| R-free | 0.24640 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1psz |
| RMSD bond length | 0.016 |
| RMSD bond angle | 1.627 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0066) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 19.800 | 2.890 |
| High resolution limit [Å] | 2.740 | 2.740 |
| Rmerge | 0.100 | 0.570 |
| Number of reflections | 28404 | |
| <I/σ(I)> | 9.3 | 1.7 |
| Completeness [%] | 99.2 | 73.1 |
| Redundancy | 3.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 33% PEG 1500, 0.15 M SPG BUFFER PH 4.0, 0.2 M MNSO4. |
