3N2U
Crystal structure of the catalytic domain of human MMP12 complexed with the inhibitor N-hydroxy-2-(4-methoxy-N(2-(3,4,5-trihydroxy-6-(hydroxymethyl)tetrahydro-2H-pyran-2-yloxy)ethyl)phenylsulfonamido)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 | 51.394, 60.446, 54.043 |
| Unit cell angles | 90.00, 114.67, 90.00 |
Refinement procedure
| Resolution | 30.220 - 1.810 |
| R-factor | 0.16585 |
| Rwork | 0.161 |
| R-free | 0.21899 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1y93 |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.210 |
| 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] | 30.220 | 1.900 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.042 | 0.115 |
| Number of reflections | 12054 | |
| <I/σ(I)> | 12.9 | 6.4 |
| Completeness [%] | 86.2 | 24.7 |
| Redundancy | 3.8 | 1.3 |
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 |
