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 |