6EKN

Crystal structure of MMP12 in complex with inhibitor BE7.

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	2016-11-23
Detector	DECTRIS EIGER X 9M
Wavelength(s)	0.980035
Spacegroup name	C 1 2 1
Unit cell lengths	51.560, 60.350, 54.560
Unit cell angles	90.00, 116.10, 90.00

Refinement procedure

Resolution	36.740 - 1.200
R-factor	0.14574
Rwork	0.144
R-free	0.17523
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4i03
RMSD bond length	0.027
RMSD bond angle	2.377
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	MOLREP
Refinement software	REFMAC (5.8.0158)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	36.740	1.230
High resolution limit [Å]	1.200	1.200
Rmeas	0.096	1.800
Number of reflections	46976	3280
<I/σ(I)>	10.21	0.98
Completeness [%]	99.3	94.7
Redundancy	6.61	6.18
CC(1/2)	0.998	0.320

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	10	293	Protein: 1 micro-L MMP12 at 290 micro-M with 10 milli-M acetohydroxamate + 0.1 Micro-L BE6 from 10 milii-M in 100% DMSO Precipitant: 17% PEG 20K, 250 milli-M NaCl, 100 milii-M TRIS HCl, pH 10.0. cryoprotectant: 40% (25 % di-ethylene glycol + 25 % glycerol + 25 % 1,2-propanediol) 10 % PEG 10K, 200 milli-M NaCl, 100 milli-M AAB (Na acetate,N-(2-Acetamido)iminodiacetic acid (ADA), Bicine) 10% acid/90% basic