1SU3
X-ray structure of human proMMP-1: New insights into collagenase action
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | MPG/DESY, HAMBURG BEAMLINE BW6 |
Synchrotron site | MPG/DESY, HAMBURG |
Beamline | BW6 |
Detector technology | CCD |
Wavelength(s) | 1.28200, 1.28380, 1.0500 |
Spacegroup name | I 4 2 2 |
Unit cell lengths | 142.746, 142.746, 295.308 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.200 |
R-factor | 0.22422 |
Rwork | 0.223 |
R-free | 0.25233 |
Structure solution method | MAD |
RMSD bond length | 0.011 |
RMSD bond angle | 1.269 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | MLPHARE |
Refinement software | REFMAC (5.1.24) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | |
High resolution limit [Å] | 2.020 | 2.020 |
Number of reflections | 72595 | |
<I/σ(I)> | 27.26 | 27.26 |
Redundancy | 5.46 | 5.46 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 1.5M Li2SO4, 0.1M Hepes, pH 7.5, VAPOR DIFFUSION, SITTING DROP |