6HKQ
Human GPX4 in complex with covalent Inhibitor ML162 (S enantiomer)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU MICROMAX-007 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2018-03-26 |
Detector | DECTRIS PILATUS 200K |
Wavelength(s) | 1.5418 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 32.734, 57.249, 81.311 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 46.810 - 1.540 |
R-factor | 0.15116 |
Rwork | 0.149 |
R-free | 0.18416 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.013 |
RMSD bond angle | 1.701 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0189) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 46.810 | 1.590 |
High resolution limit [Å] | 1.540 | 1.540 |
Rmeas | 0.110 | 0.970 |
Rpim | 0.030 | 0.330 |
Number of reflections | 20009 | 1092 |
<I/σ(I)> | 20.2 | 2.4 |
Completeness [%] | 86.6 | 72.1 |
Redundancy | 10.5 | 6.7 |
CC(1/2) | 0.810 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 | 293 | Reservoir made from 0.2 M ammonium sulfate, 20% (w/v) PEG 3350. Prio to crystal set-up, the protein was modified with covalent inhibitor, purified via gelfiltration and concentrated to 13.5 mg/ml in 50 mM TrisHCl pH 8.0, 150 mM NaCl, 5mM TCEP |