4GR0

Crystal structure of the catalytic domain of Human MMP12 in complex with selective phosphinic inhibitor RXP470B

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-1
Synchrotron site	ESRF
Beamline	ID14-1
Temperature [K]	100
Detector technology	CCD
Collection date	2010-04-24
Detector	ADSC QUANTUM 4r
Wavelength(s)	0.9334
Spacegroup name	P 21 21 2
Unit cell lengths	69.770, 62.760, 37.840
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	32.406 - 1.497
R-factor	0.188
Rwork	0.186
R-free	0.21780
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4gql
RMSD bond length	0.006
RMSD bond angle	1.107
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	1.590
High resolution limit [Å]	1.500	4.470	1.500
Rmerge	0.111	0.040	1.040
Number of reflections	26347
<I/σ(I)>	9.33	31.59	1.19
Completeness [%]	95.6	98.8	77.7
Redundancy	3.51	3.25	2.88

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	293	Protein complex: hMMP12 F171D 855 microM, inhibitor 0.788 milliM. Reservoir: 35% PEG 4,000 0.2M imidazole malate pH 8.5. Drops: 1 microL protein complex + 1 microL reservoir. Cryoprotectant: 40% MPEG 5K, 10% 1,2-propanediol, (10% (Na acetate, ADA, Bicine) 90% at pH 4/ 10% at pH 9.0). Flash freezing in Liquid N2, VAPOR DIFFUSION, SITTING DROP, temperature 293K