5I0L
Crystal structure of the catalytic domain of MMP-12 in complex with a selective sugar-conjugated arylsulfonamide carboxylate water-soluble inhibitor (DC27).
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE MASSIF-1 |
| Synchrotron site | ESRF |
| Beamline | MASSIF-1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2015-01-29 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.965 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 39.090, 62.860, 63.750 |
| Unit cell angles | 90.00, 102.54, 90.00 |
Refinement procedure
| Resolution | 44.220 - 2.450 |
| R-factor | 0.179 |
| Rwork | 0.175 |
| R-free | 0.25300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4h84 |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.754 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | REFMAC |
| Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 45.000 | 2.510 |
| High resolution limit [Å] | 2.450 | 2.450 |
| Rmerge | 0.111 | 0.230 |
| Number of reflections | 11195 | |
| <I/σ(I)> | 9.6 | 5.23 |
| Completeness [%] | 99.2 | 99.3 |
| Redundancy | 3.14 | 3.23 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 293 | Protein-inhibitor complex: hMMP12 0.631 milli-M + 0.010 M Acetohydroxamic acid + 0.005 M inhibitor DC27, 10% DMSO. precipitant: 34% PEG 4K, 1.5 M imidazole piperidine, pH 8.5, Dioxane 25% Cryoprotectant: 40% Cryomix: (12.5 % diethylene glycol + 12.5 % glycerol + 12.5 % 1,2-propanediol + 12.5 % 2,3-butanediol + 25 % DMSO + 30 % 1,4-dioxane), 25% MPEG 6K, 0.1 M AAB (Na acetate, ADA, Bicine: 10% acid/90% basic), pH 8.5 |
