6QE2
Crystal structure of Paleococcus ferrophilus monoacylglycerol lipase.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SOLEIL BEAMLINE PROXIMA 2 |
Synchrotron site | SOLEIL |
Beamline | PROXIMA 2 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2016-06-11 |
Detector | DECTRIS EIGER X 9M |
Wavelength(s) | 0.9801 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 120.600, 75.460, 85.440 |
Unit cell angles | 90.00, 128.29, 90.00 |
Refinement procedure
Resolution | 35.664 - 1.746 |
R-factor | 0.1725 |
Rwork | 0.171 |
R-free | 0.19750 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3hju |
RMSD bond length | 0.007 |
RMSD bond angle | 0.914 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | PHENIX (1.11_2563) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 35.664 | 35.664 | 1.790 |
High resolution limit [Å] | 1.746 | 7.810 | 1.750 |
Rmerge | 0.046 | 0.028 | 0.382 |
Rmeas | 0.053 | 0.033 | 0.448 |
Number of reflections | 60488 | 706 | 4104 |
<I/σ(I)> | 13.67 | 32.05 | 2.33 |
Completeness [%] | 98.6 | 95.5 | 90.7 |
Redundancy | 3.651 | 3.622 | 3.526 |
CC(1/2) | 0.999 | 0.998 | 0.936 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | MICROBATCH | 293.15 | Protein solution ( 15 mg/mL in Hepes 20 mM pH 8.1, NaCl 150 mM, LDAO 0.1 %, Glycerol 10% m/m) mixed with an equal volume of PEG 3350 20 %, potassium formate 0.2 M |