4UHH
Structural studies of a thermophilic esterase from Thermogutta terrifontis (cacodylate complex)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | DIAMOND BEAMLINE I04 |
| Synchrotron site | Diamond |
| Beamline | I04 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Detector | DECTRIS PIXEL |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 43.310, 43.310, 226.850 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 37.810 - 1.060 |
| R-factor | 0.10393 |
| Rwork | 0.103 |
| R-free | 0.12312 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2xua |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.699 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0073) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 37.810 | 1.090 |
| High resolution limit [Å] | 1.060 | 1.060 |
| Rmerge | 0.060 | 0.630 |
| Number of reflections | 113560 | |
| <I/σ(I)> | 18.5 | 2.1 |
| Completeness [%] | 99.7 | 96.2 |
| Redundancy | 8.9 | 4.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 |
