3F18
Crystal structure of the catalytic domain of human MMP12 complexed with the inhibitor 4-fluoro-N-(2-hydroxyethyl)-N-(2-nitroso-2-oxoethyl)benzenesulfonamide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE BW7A |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | BW7A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-01-21 |
| Detector | MAR CCD 165 mm |
| Wavelength(s) | 1.00800 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 51.709, 60.326, 53.992 |
| Unit cell angles | 90.00, 115.07, 90.00 |
Refinement procedure
| Resolution | 30.160 - 1.130 |
| R-factor | 0.16781 |
| Rwork | 0.166 |
| R-free | 0.18691 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.482 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 1.160 |
| High resolution limit [Å] | 1.100 | 1.100 |
| Rmerge | 0.064 | 0.303 |
| Number of reflections | 53715 | |
| <I/σ(I)> | 12.6 | 4.1 |
| Completeness [%] | 93.5 | 71 |
| Redundancy | 2.9 | 2.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8 | 293 | 0.1M TRIS, 30% PEG 6000, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
