5D3C
Crystal structure of a double mutant catalytic domain of Human MMP12 in complex with an hydroxamate analogue of RXP470
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SOLEIL BEAMLINE PROXIMA 2 |
Synchrotron site | SOLEIL |
Beamline | PROXIMA 2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2015-07-22 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.9801 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 68.640, 63.060, 36.540 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 46.438 - 1.314 |
R-factor | 0.1545 |
Rwork | 0.153 |
R-free | 0.19130 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4gql |
RMSD bond length | 0.006 |
RMSD bond angle | 1.071 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | MOLREP |
Refinement software | PHENIX (1.8_1069) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 46.438 | 1.350 |
High resolution limit [Å] | 1.310 | 1.310 |
Rmerge | 0.123 | 1.640 |
Number of reflections | 71186 | |
<I/σ(I)> | 9.47 | 1.03 |
Completeness [%] | 97.6 | 73.2 |
Redundancy | 6.83 | 3.93 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 9.5 | 293 | Protein : MMP12 F67D K241A, 1 mili-M + 10 mili-M AHA Drop : 1 micro-L protein + 0.2 micro-L inhibitor (5 mili-M in DMSO) Precipitant : 20% PEG4000, 0.2 M TRIS pH 9.5 Cryoprotectant : 10 % diethylene glycol + 5 % glycerol + 10 % 2,3-butanediol + 5 % 1,4-dioxane +25% PEG6000,+ 100 mili-M TRIS HCl, pH 8. |