3F1A
Crystal structure of the catalytic domain of human MMP12 complexed with the inhibitor 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 | 2005-07-26 |
| Detector | MAR CCD 165 mm |
| Wavelength(s) | 0.93920 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 51.834, 60.282, 54.178 |
| Unit cell angles | 90.00, 115.17, 90.00 |
Refinement procedure
| Resolution | 25.690 - 1.250 |
| R-factor | 0.16918 |
| Rwork | 0.167 |
| R-free | 0.18884 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.099 |
| 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] | 49.030 | 1.320 |
| High resolution limit [Å] | 1.250 | 1.250 |
| Rmerge | 0.052 | 0.314 |
| Number of reflections | 41409 | |
| <I/σ(I)> | 13.1 | 3.8 |
| Completeness [%] | 99.3 | 98 |
| Redundancy | 3.1 | 2.8 |
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 |
