5I4O

Crystal structure of the catalytic domain of MMP-12 in complex with a selective sugar-conjugated triazole-linked carboxylate zinc-chelator water-soluble inhibitor (DC28).

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	2014-09-24
Detector	ADSC QUANTUM 315r
Wavelength(s)	0.9801
Spacegroup name	P 1 21 1
Unit cell lengths	63.980, 63.510, 78.640
Unit cell angles	90.00, 102.31, 90.00

Refinement procedure

Resolution	32.870 - 2.050
R-factor	0.212
Rwork	0.210
R-free	0.24900
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5iol
RMSD bond length	0.020
RMSD bond angle	1.938
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]	44.560	2.000
High resolution limit [Å]	1.950	1.950
Rmerge	0.230	0.985
Number of reflections	45133
<I/σ(I)>	4.79	1.68
Completeness [%]	98.4	86.8
Redundancy	4.49	4.25

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	293	Protein-ligand: 465 micro-M hMMP12 F171D E219Q, 0.020 M acetohydroxamic acid, 10% DMSO, 0.5 milli-M inhibitor (DC28). Precipitant: 40.5% PEG4K, 10% dioxane, 2% ethylene glycol, 0.18 M imidazole piperidine, pH 8.5. Cryoprotectant:40% cryomix CM12: (,25 % diethylene glycol + 12.5 % glycerol + 25 % 1,2-propanediol + 12.5 % 1,4-dioxane), 25% PEG 6K, 0.1 M TRIS HCl, pH 8.0.