5I3M

Crystal structure of the catalytic domain of MMP-12 in complex with a selective sugar-conjugated thiourea-linked carboxylate zinc-chelator water-soluble inhibitor (DC31).

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	63.720, 63.140, 78.920
Unit cell angles	90.00, 103.09, 90.00

Refinement procedure

Resolution	48.790 - 2.170
R-factor	0.2085
Rwork	0.206
R-free	0.25324
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5i2z
RMSD bond length	0.017
RMSD bond angle	1.904
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	MOLREP
Refinement software	REFMAC (5.8.0135)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	48.790	2.230
High resolution limit [Å]	2.170	2.170
Rmerge	0.100	0.523
Number of reflections	32560
<I/σ(I)>	9.44	3.06
Completeness [%]	99.3	98.9
Redundancy	4.34	3.73
CC(1/2)	0.997

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	293	Protein-ligand: hMMP12 F67D E219Q 465 micro-M, 0.02M acetohydroxamic acid 0.5 milli-M inhibitor (DC31) 10% DMSO. Precipitant: 32.4% PEG 4K, 8% dioxane, 0.2M imidazole piperidine, pH 8.5. Cryoprotectant: 40% cryomix:(12.5 % diethylene glycol + 12.5 % glycerol + 12.5 % 1,2-propanediol + 25 % DMSO + 25 % 1,4-dioxane) 12% PEG 4K, 10% Dioxane, 0.1 M imidazole piperidine pH 8.5.