6AX1
Structure of human monoacylglycerol lipase bound to a covalent inhibitor
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 17-ID |
Synchrotron site | APS |
Beamline | 17-ID |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2013-06-02 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 1.0 |
Spacegroup name | I 2 2 2 |
Unit cell lengths | 86.360, 126.900, 137.510 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 93.260 - 2.260 |
R-factor | 0.1647 |
Rwork | 0.163 |
R-free | 0.19840 |
Structure solution method | FOURIER SYNTHESIS |
RMSD bond length | 0.010 |
RMSD bond angle | 1.080 |
Data reduction software | XDS |
Data scaling software | SCALA (3.3.16) |
Phasing software | BUSTER-TNT |
Refinement software | BUSTER (2.11.5) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 93.258 | 93.258 | 2.380 |
High resolution limit [Å] | 2.260 | 7.150 | 2.260 |
Rmerge | 0.071 | 0.428 | |
Rmeas | 0.118 | 0.086 | 0.529 |
Rpim | 0.047 | 0.035 | 0.308 |
Total number of observations | 202567 | 7347 | 9403 |
Number of reflections | 34396 | 1236 | 4041 |
<I/σ(I)> | 10.9 | 23.7 | 2.1 |
Completeness [%] | 96.4 | 99.9 | 79 |
Redundancy | 5.9 | 5.9 | 2.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 298 | Reservoir Buffer: 0.07M sodium cacodylate pH 5.1-5.9 and 33-51% MPD The protein is 20 mg/mL in a buffer of 15 mM HEPES pH 8.2; 2 mM TCEP; and 10% glycerol, with hexaethylene glycol monododecyl ether added to 0.1 mM. Apo protein crystals obtained in this manner were transferred to a cryo-protectant solution consisting of 70 mM NaCacodylate pH 5.1; 10% MPD; 30% PEG-MME-2K, and 1mM of inhibitor compound. Crystals were soaked overnight, then flash-frozen in LN2. |