4E3T
Round 18 Arylesterase Variant of Phosphotriesterase with Bound Transition State Analog
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-4 |
Synchrotron site | ESRF |
Beamline | ID14-4 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2010-11-20 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.9393 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 85.771, 85.975, 88.727 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 29.576 - 1.650 |
R-factor | 0.1749 |
Rwork | 0.173 |
R-free | 0.20550 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2r1n |
RMSD bond length | 0.021 |
RMSD bond angle | 1.894 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | MOLREP |
Refinement software | PHENIX ((phenix.refine: 1.7.1_743)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 1.740 |
High resolution limit [Å] | 1.650 | 1.650 |
Number of reflections | 79417 | |
Completeness [%] | 99.9 | 99.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 298.15 | 50mM MES, 2% PEG8000, 30% MPD, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.15K |