4H76
Crystal structure of the catalytic domain of Human MMP12 in complex with a broad spectrum hydroxamate inhibitor
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID23-1 |
Synchrotron site | ESRF |
Beamline | ID23-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2011-01-31 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.8726 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 69.920, 62.890, 37.700 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 46.758 - 1.500 |
R-factor | 0.1662 |
Rwork | 0.165 |
R-free | 0.18840 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3ljg |
RMSD bond length | 0.007 |
RMSD bond angle | 1.079 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | MOLREP |
Refinement software | PHENIX ((phenix.refine: 1.8_1069)) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 1.590 |
High resolution limit [Å] | 1.500 | 4.470 | 1.500 |
Rmerge | 0.114 | 0.044 | 1.094 |
Number of reflections | 27420 | ||
<I/σ(I)> | 14.21 | 40.9 | 2.5 |
Completeness [%] | 99.7 | ||
Redundancy | 7.98 | 7.13 | 7.92 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 293 | Protein:(hMMP12 F171D at 927 micro-M + acetohydroxamic acid at 11.6 milli-M Reservoir: 45% PEG 4,000 0.2 M imidazole piperidine Cryoprotection: 10% Di-ethylene glycol, 10% 1.2-propanediol, 10% glycerol, 10% PEG 10,000, 10% (AAB buffer 10% acid/90% basic) 0.2 M NaCl. Flash cooling in LN2. , pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K |