1RMZ
Crystal structure of the catalytic domain of human MMP12 complexed with the inhibitor NNGH at 1.3 A resolution
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ELETTRA BEAMLINE 5.2R |
| Synchrotron site | ELETTRA |
| Beamline | 5.2R |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2003-10-05 |
| Detector | MARRESEARCH |
| Wavelength(s) | 1.20000 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 69.194, 62.564, 37.262 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 1.340 |
| R-factor | 0.18111 |
| Rwork | 0.179 |
| R-free | 0.21490 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1os9 |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.668 |
| Data reduction software | MOSFLM |
| Data scaling software | CCP4 ((SCALA)) |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.1.24) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 46.407 | 1.410 |
| High resolution limit [Å] | 1.340 | 1.340 |
| Rmerge | 0.057 | 0.308 |
| Number of reflections | 36295 | |
| <I/σ(I)> | 7.2 | 2.3 |
| Completeness [%] | 98.4 | 92.6 |
| Redundancy | 6.2 | 4.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8 | 293 | Tris, PEG6000, NNGH, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
