4H49

Crystal structure of the catalytic domain of MMP-12 in complex with a twin inhibitor.

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	2012-07-04
Detector	DECTRIS PILATUS 6M
Wavelength(s)	0.98011
Spacegroup name	P 1 21 1
Unit cell lengths	47.440, 106.490, 65.880
Unit cell angles	90.00, 94.96, 90.00

Refinement procedure

Resolution	47.262 - 2.160
R-factor	0.1703
Rwork	0.167
R-free	0.24070
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4h30
RMSD bond length	0.008
RMSD bond angle	1.104
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	2.290
High resolution limit [Å]	2.160	6.420	2.160
Rmerge	0.112	0.049	0.696
Number of reflections	34818
<I/σ(I)>	12.21	32.67	2.6
Completeness [%]	99.3	99.6	96
Redundancy	5.63	5.4	5.46

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6	293	Protein: hMMP12 F171D 0.78 milli-M + 0.010 M AHA. Reservoir: 17% PEG 20.000, 0.2 M imidazole malate, pH 6.0, 0.25 M NaCl. Cryoprotectant: 10% di-ethylene glycol + 10% glycerol + 10% 1,2-propanediol, 25% M PEG 5.000, 0.1 M BES pH 5.5., VAPOR DIFFUSION, SITTING DROP, temperature 293K