4H82
Crystal structure of mutant MMP-9 catalytic domain in complex with a twin inhibitor.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SOLEIL BEAMLINE PROXIMA 1 |
| Synchrotron site | SOLEIL |
| Beamline | PROXIMA 1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2012-07-04 |
| Detector | DECTRIS PILATUS 6M |
| Spacegroup name | P 1 |
| Unit cell lengths | 39.900, 98.860, 47.130 |
| Unit cell angles | 90.03, 111.95, 89.98 |
Refinement procedure
| Resolution | 33.460 - 1.900 |
| R-factor | 0.209 |
| Rwork | 0.207 |
| R-free | 0.24100 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4h1q |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.233 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | MOLREP |
| Refinement software | PHENIX ((phenix.refine: 1.8_1069)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.020 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.132 | 0.773 |
| Number of reflections | 45622 | |
| <I/σ(I)> | 6.35 | 1.21 |
| Completeness [%] | 86.8 | 68.6 |
| Redundancy | 2.25 | 2.17 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 8 | 293 | Protein: MMP9h Nter=GFQT E402Q V391Q at 384.3 micro-M with 120 milli-M AHA Reservoir: 10% MPEG 20K, 100mM PCTP 75/25, 1.5 NaCl. Cryoprotectant: 12.5% di-ethylene glycol, 12.5% DMSO, 12.5% MPD, 12.5% 1,2-propnaediol, 25% glycerol, 9% PEG 10K, 100 milli-M PCTP 80/20, 1.5 NaCl , pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
