4EFS

Human MMP12 in complex with 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	2012-02-17
Detector	PSI PILATUS 6M
Wavelength(s)	0.918400
Spacegroup name	P 21 21 2
Unit cell lengths	68.970, 63.190, 37.510
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	46.590 - 1.630
R-factor	0.15554
Rwork	0.154
R-free	0.19044
Structure solution method	RIGID BODY
Starting model (for MR)	3lik
RMSD bond length	0.029
RMSD bond angle	2.607
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	REFMAC (5.5.0109)
Refinement software	REFMAC (5.5.0109)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	46.590	46.590	1.720
High resolution limit [Å]	1.630	4.860	1.630
Rmerge	0.086	0.037	0.726
Number of reflections	20710
<I/σ(I)>	18.72	48.38	3.31
Completeness [%]	97.4	99.7	99.3
Redundancy	8.72	7.49	8.55

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	293	Protein solution - 0.53 mM F67D mutant of human MMP12 residues 106-263 in 0.1 M acetohydroxamic acid 0.003 M CaCl2, 0.200 M NaCl 0.02 M Tris-HCl, pH 7.5. Reservoir solution -27% PEG 10K,0.2 M imidazole malate cryoconditions - CryoProtX-Cryomix 7, 25% MPEG 5K, 0.1 M AAB 10/90, VAPOR DIFFUSION, SITTING DROP, temperature 293.0K