2Y6Y
Crystal structure of TtrD from Archaeoglobus fulgidus
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-02-13 |
| Detector | ADSC CCD |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 87.058, 87.058, 83.392 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 55.930 - 2.200 |
| R-factor | 0.21805 |
| Rwork | 0.217 |
| R-free | 0.23767 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2xol |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.130 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 55.900 | 2.320 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.110 | 0.390 |
| Number of reflections | 18960 | |
| <I/σ(I)> | 14.1 | 3.5 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 9.9 | 4.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | PROTEIN BUFFER 50 MM TRIS, 250 MM NACL, PH 7.5; RESERVOIR 4.3 M NACL, 0.1 M HEPES PH 7.5. |
