2OXW
Human MMP-12 complexed with the peptide IAG
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-4 |
Synchrotron site | ESRF |
Beamline | ID14-4 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-05-17 |
Detector | ADSC QUANTUM 315 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 51.888, 60.358, 54.521 |
Unit cell angles | 90.00, 115.73, 90.00 |
Refinement procedure
Resolution | 36.960 - 1.150 |
R-factor | 0.19942 |
Rwork | 0.197 |
R-free | 0.22250 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1y93 |
RMSD bond length | 0.007 |
RMSD bond angle | 1.093 |
Data reduction software | MOSFLM |
Data scaling software | CCP4 ((SCALA)) |
Phasing software | MOLREP |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 49.080 | 1.210 |
High resolution limit [Å] | 1.150 | 1.150 |
Rmerge | 0.059 | 0.156 |
Number of reflections | 50850 | |
<I/σ(I)> | 4.2 | 4.1 |
Completeness [%] | 94.6 | 91.1 |
Redundancy | 6.8 | 6.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8 | 298 | 0.1 M Tris-HCl, 30% PEG6000, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 298K |