4H30

Crystal structure of the catalytic domain of MMP-12 in complex with a twin 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	2012-05-01
Detector	DECTRIS PILATUS 6M
Wavelength(s)	0.8856
Spacegroup name	P 21 21 21
Unit cell lengths	46.910, 61.750, 112.560
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	43.310 - 1.430
R-factor	0.1577
Rwork	0.157
R-free	0.17670
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4efs
RMSD bond length	0.006
RMSD bond angle	1.118
Data reduction software	XDS
Data scaling software	XDS
Phasing software	MOLREP
Refinement software	PHENIX ((phenix.refine: 1.8_1069))

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	1.510
High resolution limit [Å]	1.430	4.250	1.420
Rmerge	0.059	0.027	0.626
Number of reflections	61752
<I/σ(I)>	19.29	57.77	2.77
Completeness [%]	99.7	99.5	98.4
Redundancy	5.82	5.19	5.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	293	Protein: hMMP12 F171D at 0.36 milli-M + 0.001 M AHA. Reservoir: 13% PEG 20,000 0.2 M imidazole malate 0.05 M NaCl Cryoprotectant: 27% PEG 8,000 15% MPEG 550, 10% glycerol, 0.09 M Tris-HCl , pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K