3N2V
Crystal structure of the catalytic domain of human MMP12 complexed with the inhibitor N-hydroxy-2-(N-hydroxyethyl)biphenyl-4-ylsulfonamido)acetamide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SEALED TUBE |
| Source details | OXFORD DIFFRACTION ENHANCE ULTRA |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2003-10-28 |
| Detector | OXFORD ONYX CCD |
| Wavelength(s) | 1.54056 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 51.614, 60.277, 54.186 |
| Unit cell angles | 90.00, 115.20, 90.00 |
Refinement procedure
| Resolution | 14.440 - 1.550 |
| R-factor | 0.13619 |
| Rwork | 0.132 |
| R-free | 0.18020 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1y93 |
| RMSD bond length | 0.025 |
| RMSD bond angle | 1.833 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 14.440 | 1.630 |
| High resolution limit [Å] | 1.550 | 1.550 |
| Rmerge | 0.042 | 0.212 |
| Number of reflections | 21123 | |
| <I/σ(I)> | 11.2 | 3.5 |
| Completeness [%] | 96.7 | 82.3 |
| Redundancy | 2 | 1.2 |
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 |
