5CXA

Crystal structure of the catalytic domain of Human MMP12 in complex with a carboxylate inhibitor related to RXP470

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID23-2
Synchrotron site	ESRF
Beamline	ID23-2
Temperature [K]	100
Detector technology	PIXEL
Collection date	2014-09-07
Detector	DECTRIS PILATUS 6M
Wavelength(s)	0.8729
Spacegroup name	P 21 21 2
Unit cell lengths	69.230, 63.700, 36.620
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	36.620 - 1.300
R-factor	0.1423
Rwork	0.140
R-free	0.18100
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4gql
RMSD bond length	0.005
RMSD bond angle	0.848
Data reduction software	XDS
Data scaling software	XDS
Phasing software	MOLREP
Refinement software	PHENIX ((1.10.1_2155: ???))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	46.880	1.380
High resolution limit [Å]	1.300	1.300
Rmerge	0.165	1.390
Number of reflections	40584
<I/σ(I)>	9.23	1.24
Completeness [%]	99.9	99.3
Redundancy	9.05	8.67

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	10	293	Protein: hMMP12 F171D K241A at 608 micro-M + 10 milli-M AHA + 0.552 milli-M inhibitor. precipitant: 26% PEG4000, 3% dioxane, 0.114 M TRIS pH 10. cryoprotectant: 10 % diethylene glycol + 5 % glycerol + 10 % 2,3-butanediol + 5 % 1,4-dioxane, 25% PEG 6K, 0.1 M TRIS-HCl, pH 8.0