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 |