5I43

Crystal structure of the catalytic domain of MMP-12 in complex with a selective sugar-conjugated triazole-linked carboxylate chelator water-soluble inhibitor (DC32).

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	64.030, 63.660, 79.030
Unit cell angles	90.00, 103.03, 90.00

Refinement procedure

Resolution	44.560 - 1.950
R-factor	0.20205
Rwork	0.200
R-free	0.23323
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5i3m
RMSD bond length	0.021
RMSD bond angle	1.989
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	0.172	0.716
Number of reflections	45366
<I/σ(I)>	7.24	2.02
Completeness [%]	99.9	99.8
Redundancy	5.97	3.96
CC(1/2)	0.993

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	295	Protein-ligand: hMMP12 F171D E219Q 465 micro-M in 0.020 M Tris-HCl, 3 milli-M CaCl2, 0.2 M NaCl, 0.02 M acetohydroxamic acid, 10% DMSO, pH 7.5, 0.5 milli-M inhibitor (DC31). Precipitant: 40% PEG4K, 9% dioxane, 0.18 M imidazole piperidine, pH 8.5. Cryoprotectant: 40% cryomix SM2:(12.5 % ethylene glycol + 12.5 % glycerol + 12.5 % 1,2-propanediol + 25 % DMSO + 37.5 % 1,4-dioxane), 22.5% MPEG 4K, 5% dioxane, 100 mM imidazole piperidine pH 8.5.