6FR2
Soluble epoxide hydrolase in complex with LK864
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID29 |
Synchrotron site | ESRF |
Beamline | ID29 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2017-09-16 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 1.072 |
Spacegroup name | I 2 2 2 |
Unit cell lengths | 80.091, 92.180, 106.998 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 46.090 - 2.262 |
R-factor | 0.1698 |
Rwork | 0.168 |
R-free | 0.21000 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4jnc |
RMSD bond length | 0.011 |
RMSD bond angle | 0.955 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | PHASER |
Refinement software | PHENIX (1.12_2829) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 46.090 | 46.090 | 2.300 |
High resolution limit [Å] | 2.260 | 20.000 | 2.260 |
Rmerge | 0.081 | 0.052 | 0.788 |
Rmeas | 0.096 | 0.062 | 0.955 |
Total number of observations | 120149 | ||
Number of reflections | 35335 | 48 | 1497 |
<I/σ(I)> | 9.4 | 21.89 | 1.71 |
Completeness [%] | 98.5 | 88.9 | 82.7 |
Redundancy | 3.4 | 3.021 | 2.983 |
CC(1/2) | 0.996 | 0.995 | 0.779 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 277 | 1 uL protein solution Protein (5-10 mg/mL , 50 mM NaCl, 50 mM sodium phosphate, 10% glycerol (98%), 2 mM DTT at pH 7.4) was mixed in different ratios (2/1, 1/1, 1/2) with precipitant solution (23 %-28 % (w/v) polyethylenglycol (PEG) 6000, 70 mM ammonium acetat, 200 mM magnesium acetat, 100 mM sodium cacodylate at pH 6.1-6.5) |