5D2B
Crystal structure of a mutated catalytic domain of Human MMP12 in complex with an hydroxamate analogue of RXP470
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 | CCD |
| Collection date | 2015-07-22 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9184 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 68.900, 63.100, 36.790 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 32.453 - 1.200 |
| R-factor | 0.1554 |
| Rwork | 0.154 |
| R-free | 0.17470 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4gql |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.067 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | MOLREP |
| Refinement software | PHENIX (1.8_1069) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 32.453 | 1.230 |
| High resolution limit [Å] | 1.200 | 1.200 |
| Rmerge | 0.100 | 1.050 |
| Number of reflections | 96542 | |
| <I/σ(I)> | 8.78 | 1.53 |
| Completeness [%] | 99.6 | 96.9 |
| Redundancy | 4.6 | 2.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 9.5 | 293 | Protein : hMMP12 F171D at 820 micro-M + 10 milli-M AHA + 0.708 milli-M inhibitor. Precipitant : 20% PEG4000, 0.2 M TRIS pH 9.5 Cryoprotectant : 10 % diethylene glycol + 5 % glycerol + 10 % 1,2-propanediol + 5 % 1,4-dioxane + 25% PEG6000 + 0.1 M TRIS HCl pH 8.0 |
