1OS9
Binary enzyme-product complexes of human MMP12
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-1 |
| Synchrotron site | ESRF |
| Beamline | ID14-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2003-02-01 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.9322 |
| Spacegroup name | P 31 |
| Unit cell lengths | 125.445, 125.445, 72.339 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 19.800 * - 1.850 |
| R-factor | 0.19771 |
| Rwork | 0.195 |
| R-free | 0.24000 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1jk3 |
| RMSD bond length | 0.020 * |
| RMSD bond angle | 1.900 * |
| Data reduction software | MOSFLM |
| Data scaling software | CCP4 ((SCALA)) |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.1.80) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 47.400 * | 1.950 |
| High resolution limit [Å] | 1.850 | 1.850 |
| Rmerge | 0.083 | 0.474 |
| Total number of observations | 363460 * | |
| Number of reflections | 108393 * | |
| <I/σ(I)> | 6.7 | 1.8 |
| Completeness [%] | 99.9 | 99.7 |
| Redundancy | 3.4 | 3.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion * | 8 | 20 * | Tris, PEG6000, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | Tris-HCl | 0.1 (M) | |
| 2 | 1 | reservoir | PEG6000 | 30 (%) | |
| 3 | 1 | reservoir | AHA | 200 (mM) | pH8.0 |
| 4 | 1 | drop | protein | 8 (mg/ml) |
