4GR3

Crystal structure of the catalytic domain of Human MMP12 in complex with selective phosphinic inhibitor RXP470A

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-2
Synchrotron site	ESRF
Beamline	ID14-2
Temperature [K]	100
Detector technology	CCD
Collection date	2009-09-20
Detector	ADSC QUANTUM 4
Wavelength(s)	0.9334
Spacegroup name	P 21 21 2
Unit cell lengths	68.960, 63.130, 37.310
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	46.565 - 1.494
R-factor	0.1821
Rwork	0.180
R-free	0.21580
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4gql
RMSD bond length	0.006
RMSD bond angle	1.091
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	1.580
High resolution limit [Å]	1.490	4.460	1.490
Rmerge	0.106	0.032	1.170
Number of reflections	27049
<I/σ(I)>	16.12	56.41	1.97
Completeness [%]	99.7	99.4	98.9
Redundancy	7.9	6.16	6.98

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8	293	Protein: hMMP12(F171D) 643 microM. Reservoir: 18% PEG 10000, 0.2 M imidazole malate pH 8.0. Cryoprotectant: 27% PEG 8000, 15% monomethylPEG 550, 10% glycerol, 0.09 M Tris-HCl, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K