4H30
Crystal structure of the catalytic domain of MMP-12 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 | 2012-05-01 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 0.8856 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 46.910, 61.750, 112.560 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 43.310 - 1.430 |
R-factor | 0.1577 |
Rwork | 0.157 |
R-free | 0.17670 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4efs |
RMSD bond length | 0.006 |
RMSD bond angle | 1.118 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | MOLREP |
Refinement software | PHENIX ((phenix.refine: 1.8_1069)) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 1.510 |
High resolution limit [Å] | 1.430 | 4.250 | 1.420 |
Rmerge | 0.059 | 0.027 | 0.626 |
Number of reflections | 61752 | ||
<I/σ(I)> | 19.29 | 57.77 | 2.77 |
Completeness [%] | 99.7 | 99.5 | 98.4 |
Redundancy | 5.82 | 5.19 | 5.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 293 | Protein: hMMP12 F171D at 0.36 milli-M + 0.001 M AHA. Reservoir: 13% PEG 20,000 0.2 M imidazole malate 0.05 M NaCl Cryoprotectant: 27% PEG 8,000 15% MPEG 550, 10% glycerol, 0.09 M Tris-HCl , pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K |