5I2Z

Crystal structure of the catalytic domain of MMP-12 in complex with a selective sugar-conjugated triazole-linked carboxylate chelating water-soluble inhibitor (DC24).

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	2015-04-08
Detector	DECTRIS PILATUS 6M
Wavelength(s)	0.97857
Spacegroup name	P 1 21 1
Unit cell lengths	63.990, 63.120, 78.750
Unit cell angles	90.00, 102.37, 90.00

Refinement procedure

Resolution	44.410 - 2.300
R-factor	0.217
Rwork	0.214
R-free	0.26300
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5iol
RMSD bond length	0.010
RMSD bond angle	1.422
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	MOLREP
Refinement software	PHENIX (1.9_1692)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	48.790	2.350
High resolution limit [Å]	2.290	2.290
Rmerge	0.183	0.539
Number of reflections	27728
<I/σ(I)>	6.53	2.96
Completeness [%]	99.7	100
Redundancy	4.6	4.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	293	Protein-ligand: hMMP12 F67D E219Q at 465 micro-M, 20 milli-M acetohydroxamic acid in 0.020M Tris-HCl, 3 milli-M CaCl2, 0.2M NaCl, pH 7.5, 0.2 milli-M inhibitor (DC24) 10% DMSO Precipitant: 35% PEG4K, 0.2M imidazole piperidine, 15% dioxane, pH 8.5. Cryoprotectant: 40% cryomix: (25 % diethylene glycol + 12.5 % glycerol + 25 % 1,2-propanediol + 12.5 % 1,4-dioxane) 25% PEG 6K, 100mM TRIS HCl, pH 8.0