4HMA
Crystal structure of an MMP twin carboxylate based inhibitor LC20 in complex with the MMP-9 catalytic domain
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SOLEIL BEAMLINE PROXIMA 1 |
Synchrotron site | SOLEIL |
Beamline | PROXIMA 1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2012-10-12 |
Detector | PSI PILATUS 6M |
Wavelength(s) | 0.98011 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 73.870, 98.240, 47.440 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 42.720 - 1.940 |
R-factor | 0.21439 |
Rwork | 0.211 |
R-free | 0.28302 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4h82 |
RMSD bond length | 0.022 |
RMSD bond angle | 1.966 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | MOLREP |
Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 2.060 |
High resolution limit [Å] | 1.940 | 5.790 | 1.940 |
Rmerge | 0.166 | 0.056 | 1.533 |
Number of reflections | 26019 | ||
<I/σ(I)> | 8.19 | 23.21 | 1.3 |
Completeness [%] | 99.4 | 99.5 | 96.6 |
Redundancy | 7.98 | 7.15 | 7.87 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6 | 293 | Protein: human MMP9 (E402Q) at 308.7 micro-M twin inhibitor LC20 at 154 micro-M (stoichiometry 2:1) and 120mM acetohydroxamic acid. RESERVOIR: 12% Polyethylene glycol 20,000, 1.5M NaCl, 0.1 M PCTP (Na propionate, Na cacodylate, Bis-Tris-propane ratio 2:1:2; 75% pH 4, 25% pH 9.5) CRYOPROTECTANT: 40% C2 (25 % di-ethylene glycol + 25 % glycerol + 25 % 1,2-propanediol), 9% PEG 10,000 1.5M NaCl, 0.1M PCTP 80/2, VAPOR DIFFUSION, SITTING DROP, temperature 293K |