4LZP
Structure of the TIR domain of the immunosuppressor BtpA from Brucella
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-1 |
| Synchrotron site | ESRF |
| Beamline | ID23-1 |
| Temperature [K] | 173 |
| Detector technology | CCD |
| Collection date | 2011-09-30 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.976260 |
| Spacegroup name | P 2 21 21 |
| Unit cell lengths | 68.143, 73.928, 137.645 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 48.400 - 3.150 |
| R-factor | 0.2252 |
| Rwork | 0.222 |
| R-free | 0.27870 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3h16 |
| RMSD bond length | 0.009 |
| RMSD bond angle | 0.992 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | PHASER |
| Refinement software | PHENIX ((phenix.refine: 1.8.2_1309)) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 48.400 | 48.420 | 3.320 |
| High resolution limit [Å] | 3.150 | 9.960 | 3.150 |
| Rmerge | 0.169 | 0.035 | 0.668 |
| Number of reflections | 43030 | ||
| <I/σ(I)> | 13.7 | 1.5 | |
| Completeness [%] | 98.1 | 93.8 | 99.2 |
| Redundancy | 3.2 | 3.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | EVAPORATION | 5.5 | 293 | 20% Peg4K, 100mM Na Acetate, 200mM ammonium acetate, pH 5.5, EVAPORATION, temperature 293K |
