2OXZ
Human MMP-12 in complex with two peptides PQG and IAG
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SEALED TUBE |
Source details | OTHER |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-06-05 |
Detector | KODAK |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 51.546, 60.378, 54.449 |
Unit cell angles | 90.00, 115.41, 90.00 |
Refinement procedure
Resolution | 30.190 - 1.900 |
R-factor | 0.21406 |
Rwork | 0.207 |
R-free | 0.28767 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1y93 |
RMSD bond length | 0.021 |
RMSD bond angle | 1.860 |
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] | 30.190 | 2.000 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.137 | 0.327 |
Number of reflections | 11726 | |
<I/σ(I)> | 4.7 | 2.3 |
Completeness [%] | 98.1 | 98.1 |
Redundancy | 5.6 | 3 |
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 |