1JK3
Crystal structure of human MMP-12 (Macrophage Elastase) at true atomic resolution
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | MPG/DESY, HAMBURG BEAMLINE BW6 |
| Synchrotron site | MPG/DESY, HAMBURG |
| Beamline | BW6 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2000-04-10 |
| Detector | MARRESEARCH |
| Wavelength(s) | 1.0503 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 51.905, 60.263, 54.612 |
| Unit cell angles | 90.00, 114.65, 90.00 |
Refinement procedure
| Resolution | 22.360 - 1.090 |
| R-factor | 0.16881 |
| Rwork | 0.167 |
| R-free | 0.19572 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1uea |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.875 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 22.360 | 1.130 |
| High resolution limit [Å] | 1.090 | 1.090 |
| Rmerge | 0.063 * | 0.256 * |
| Total number of observations | 359642 * | |
| Number of reflections | 60360 | |
| <I/σ(I)> | 12.68 | 3.2 |
| Completeness [%] | 95.0 | 91.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 * | 273 | LiCl, MES, pH 6.4, VAPOR DIFFUSION, SITTING DROP at 273K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | cdMMP-12 | 4 (mg/ml) | |
| 2 | 1 | drop | batimastat | 1 (mg/ml) | |
| 3 | 1 | drop | inhibitor | 1*10-6 (mM) | |
| 4 | 1 | drop | Tris | 5 (mM) | |
| 5 | 1 | drop | 50 (mM) | ||
| 6 | 1 | drop | 5 (mM) | ||
| 7 | 1 | reservoir | MES | 100 (mM) | |
| 8 | 1 | reservoir | 100 (mM) |
