5LAB
Crystal structure of the catalytic domain of human MMP12 complexed with the inhibitor NNGH
Replaces: 1RMZExperimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ELETTRA BEAMLINE 5.2R |
Synchrotron site | ELETTRA |
Beamline | 5.2R |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2003-10-05 |
Detector | MARRESEARCH |
Wavelength(s) | 1.2000 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 69.190, 62.560, 37.260 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 1.340 |
R-factor | 0.15789 |
Rwork | 0.155 |
R-free | 0.19450 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1os9 |
RMSD bond length | 0.035 |
RMSD bond angle | 1.803 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | MOLREP |
Refinement software | REFMAC (5.8.0103) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 46.407 | 1.410 |
High resolution limit [Å] | 1.340 | 1.340 |
Rmerge | 0.308 | |
Number of reflections | 36295 | |
<I/σ(I)> | 7.2 | 2.3 |
Completeness [%] | 98.4 | 92.6 |
Redundancy | 6.2 | 4.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8 | 293 | Tris, PEG6000, NNGH, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K |