6ELA

Crystal structure of MMP12 in complex with inhibitor BE4.

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	PIXEL
Collection date	2016-06-30
Detector	DECTRIS EIGER X 9M
Wavelength(s)	0.976254
Spacegroup name	P 1 21 1
Unit cell lengths	64.190, 63.320, 78.320
Unit cell angles	90.00, 103.73, 90.00

Refinement procedure

Resolution	38.041 - 1.485
R-factor	0.1732
Rwork	0.171
R-free	0.20670
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5i4o
RMSD bond length	0.005
RMSD bond angle	0.795
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	MOLREP
Refinement software	PHENIX ((1.12_2829: ???))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	43.440	1.570
High resolution limit [Å]	1.480	1.480
Rmeas	0.137	0.850
Number of reflections	100074	15656
<I/σ(I)>	7.85	1.68
Completeness [%]	99.4	96.4
Redundancy	6.67	6.51
CC(1/2)	0.997	0.874

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	293	protein solution: hMMP12 at 314 micro-M + 10 milli-M acetohydroxamate + 1 milli-M BE4, 10% DMSO precipitant: 38% PEG 4K, 0.16 M imidazole piperidine,15% Dioxane, pH 8.5. Cryoprotectant: 40% CM15 (12.5 % diethylene glycol + 12.5 % ethylene glycol + 12.5 % MPD + 12.5 % glycerol + 12.5 % 1,2-propanediol + 12.5 % 1,4-dioxane + 12.5 mM NDSB 201), 25% PEG 6K, 100 milli-M TRIS HCl, pH 7.0