4H2E
Crystal structure of an MMP twin inhibitor complexing two MMP-9 catalytic domains
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 | CCD |
| Collection date | 2010-12-20 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.98011 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 40.180, 97.400, 45.690 |
| Unit cell angles | 90.00, 111.99, 90.00 |
Refinement procedure
| Resolution | 38.850 - 2.902 |
| R-factor | 0.279 |
| Rwork | 0.277 |
| R-free | 0.31140 |
| Structure solution method | MOLREP |
| Starting model (for MR) | 4h1q |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.458 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | MOLREP |
| Refinement software | PHENIX ((phenix.refine: 1.8_1069)/REFMAC) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 3.080 |
| High resolution limit [Å] | 2.900 | 8.580 | 2.900 |
| Rmerge | 0.195 | 0.073 | 0.530 |
| Number of reflections | 7158 | ||
| <I/σ(I)> | 7.01 | 14.84 | 2.9 |
| Completeness [%] | 98.0 | 97.6 | 96.5 |
| Redundancy | 4.15 | 4 | 4.12 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 293 | protein: hMMP-9-WT at 2 mg/mL with 120 milli-M acetohydroxamic acid. Reservoir: 40% monomethyl PEG 5,000, 0.1 M glycine. Cryoprotectant: 35% MPEG 5K, 15% PEG 400, 15% AAB buffer at pH 8.0 , VAPOR DIFFUSION, SITTING DROP, temperature 293K |
