1Q3A
Crystal structure of the catalytic domain of human matrix metalloproteinase 10
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2003-04-04 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.9330 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 117.152, 61.141, 68.588 |
| Unit cell angles | 90.00, 108.68, 90.00 |
Refinement procedure
| Resolution | 51.300 - 2.100 |
| R-factor | 0.27785 |
| Rwork | 0.276 |
| R-free | 0.29797 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1g49 |
| RMSD bond length | 0.024 |
| RMSD bond angle | 2.247 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.1.24) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.210 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Rmerge | 0.140 | 0.380 |
| Number of reflections | 25246 | |
| <I/σ(I)> | 3.6 | 1.8 |
| Completeness [%] | 89.1 | |
| Redundancy | 3 | 2.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8 | 293 | Tris-HCl, PEG 6000, Acetohydroxamic acid, NNGH, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
