1GKD
MMP9 active site mutant-inhibitor complex
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SRS BEAMLINE PX9.6 |
Synchrotron site | SRS |
Beamline | PX9.6 |
Temperature [K] | 298 |
Detector technology | CCD |
Collection date | 2000-08-22 |
Detector | ADSC CCD |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 56.523, 56.523, 263.761 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 36.300 - 2.100 |
Rwork | 0.212 |
R-free | 0.25600 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | WILD-TYPE MMP-9 STRUCTURE (1GKC) |
RMSD bond length | 0.006 |
RMSD bond angle | 23.000 * |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | AMoRE |
Refinement software | CNX (2000) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 36.300 | 2.270 |
High resolution limit [Å] | 2.100 | 2.100 |
Rmerge | 0.147 | 0.385 |
Total number of observations | 50609 * | |
Number of reflections | 18276 | 2038 * |
<I/σ(I)> | 7.5 | 2.5 |
Completeness [%] | 71.2 * | 40.4 * |
Redundancy | 2.7 | 1.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 7.5 * | 15 * | PROTEIN SOLUTION (4MG/ML IN 20MM TRIS-HCL PH 7.5, 50MM NACL) WAS INCUBATED WITH 5MM INHIBITOR FOR 30MINS PRIOR TO SETTING UP CRYSTALLISATION TRIALS. THE CRYSTALLISATION DROPS CONTAINED A 1:1 MIXTURE OF COMPLEX SOLUTION AND RESERVOIR BUFFER (2.6 - 2.8 M NACL, 0.1 M HEPES PH 9.0). |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 4 (mg/ml) | |
2 | 1 | drop | Tris-HCl | 20 (mM) | pH7.5 |
3 | 1 | drop | 50 (mM) | ||
4 | 1 | drop | inhibitor | 5.0 (mM) | |
5 | 1 | reservoir | 2.6-2.8 (M) | ||
6 | 1 | reservoir | HEPES | 0.1 (M) | pH9.0 |