2OW9
Crystal structure analysis of the MMP13 catalytic domain in complex with specific inhibitor
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 17-ID |
| Synchrotron site | APS |
| Beamline | 17-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2000-03-05 |
| Detector | MAR CCD 165 mm |
| Wavelength(s) | 1.00000 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 140.764, 36.343, 71.684 |
| Unit cell angles | 90.00, 93.53, 90.00 |
Refinement procedure
| Resolution | 70.710 - 1.740 |
| R-factor | 0.168 |
| Rwork | 0.167 |
| R-free | 0.19100 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1ciz |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.043 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 70.710 | 1.780 |
| High resolution limit [Å] | 1.740 | 1.740 |
| Number of reflections | 37780 | |
| <I/σ(I)> | 17.7 | 1.9 |
| Completeness [%] | 96.5 | 67.5 |
| Redundancy | 2.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 295 | Protein concentration: 7-20 mg/ml. Well solution: 18-22% PEG MME 5000, 0.2M Lithium sulfate, 0.1M Hepes buffer. 2-4 microliter drops with 1:1 ratio of protein complex solution and well solution, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K |
