1GKC
MMP9-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 | 1999-08-25 |
Detector | ADSC CCD |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 56.005, 56.005, 262.655 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 51.300 - 2.300 |
Rwork | 0.207 |
R-free | 0.23900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1hfs |
RMSD bond length | 0.006 |
RMSD bond angle | 23.400 * |
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] | 51.300 | 2.440 |
High resolution limit [Å] | 2.300 | 2.300 |
Rmerge | 0.117 | 0.479 |
Total number of observations | 77726 * | |
Number of reflections | 17375 | 2656 * |
<I/σ(I)> | 14.4 | 4.2 |
Completeness [%] | 88.3 * | 83.3 * |
Redundancy | 4.5 | 4.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 7.5 | 15 * | THE CRYSTALLISATION DROPS CONTAINED A 1:1 MIXTURE OF PURIFIED COMPLEX SOLUTION (0.55 MG/ML PROTEIN AND 0.5 MM INHIBITOR SOLUTION CONCENTRATED TO ~4 MG/ML IN 20 MM TRIS- HCL PH 7.5, 2 MM CACL2, 50 MM NACL) AND RESERVOIR BUFFER (3.6 M NACL, 0.1 M HEPES PH 7.5). |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 0.55 (mg/ml) | |
2 | 1 | drop | inhibitor | 0.5 (mM) | |
3 | 1 | drop | Tris-HCl | 20 (mM) | pH7.5 |
4 | 1 | drop | 2 (mM) | ||
5 | 1 | drop | 50 (mM) | ||
6 | 1 | reservoir | 3.6 (M) | ||
7 | 1 | reservoir | HEPES | 0.1 (M) | pH7.5 |