5I4O
Crystal structure of the catalytic domain of MMP-12 in complex with a selective sugar-conjugated triazole-linked carboxylate zinc-chelator water-soluble inhibitor (DC28).
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 | 2014-09-24 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.9801 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 63.980, 63.510, 78.640 |
Unit cell angles | 90.00, 102.31, 90.00 |
Refinement procedure
Resolution | 32.870 - 2.050 |
R-factor | 0.212 |
Rwork | 0.210 |
R-free | 0.24900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5iol |
RMSD bond length | 0.020 |
RMSD bond angle | 1.938 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | MOLREP |
Refinement software | REFMAC (5.8.0135) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 44.560 | 2.000 |
High resolution limit [Å] | 1.950 | 1.950 |
Rmerge | 0.230 | 0.985 |
Number of reflections | 45133 | |
<I/σ(I)> | 4.79 | 1.68 |
Completeness [%] | 98.4 | 86.8 |
Redundancy | 4.49 | 4.25 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 293 | Protein-ligand: 465 micro-M hMMP12 F171D E219Q, 0.020 M acetohydroxamic acid, 10% DMSO, 0.5 milli-M inhibitor (DC28). Precipitant: 40.5% PEG4K, 10% dioxane, 2% ethylene glycol, 0.18 M imidazole piperidine, pH 8.5. Cryoprotectant:40% cryomix CM12: (,25 % diethylene glycol + 12.5 % glycerol + 25 % 1,2-propanediol + 12.5 % 1,4-dioxane), 25% PEG 6K, 0.1 M TRIS HCl, pH 8.0. |