4I03

Human MMP12 in complex with a PEG-linked bifunctional L-glutamate motif inhibitor

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	2012-10-12
Detector	PSI PILATUS 6M
Wavelength(s)	0.980110
Spacegroup name	C 1 2 1
Unit cell lengths	51.790, 60.100, 54.920
Unit cell angles	90.00, 116.67, 90.00

Refinement procedure

Resolution	36.670 - 1.700
R-factor	0.14626
Rwork	0.144
R-free	0.19397
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.022
RMSD bond angle	2.038
Data reduction software	XDS
Data scaling software	XDS
Phasing software	MOLREP
Refinement software	REFMAC (5.5.0109)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	1.800
High resolution limit [Å]	1.700	5.070	1.700
Rmerge	0.102	0.055	0.887
Number of reflections	16663
<I/σ(I)>	9.52	25.83	1.71
Completeness [%]	99.2	99.2	97.2
Redundancy	4.14	3.99	4.02

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	293	Protein solution: 222 microM MMP12 mutant E219A 106 microM bifunctional inhibitor LD884. Reservoir: 27% PEG 10K, 150mM imidazole piperidine, pH 8.5. Cryoprotectant: 5 % di-ethylene glycol + 5 % ethylene glycol + 10 % 1,2-propanediol + 5 % DMSO + 5 % glycerol, 25% MPEG 5K, 100mM (Na acetate, ADA, Bicine 10% pH 4.0/90% pH 9.0), VAPOR DIFFUSION, SITTING DROP, temperature 293K