5D3C

Crystal structure of a double mutant catalytic domain of Human MMP12 in complex with an hydroxamate analogue of RXP470

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SOLEIL BEAMLINE PROXIMA 2
Synchrotron site	SOLEIL
Beamline	PROXIMA 2
Temperature [K]	100
Detector technology	CCD
Collection date	2015-07-22
Detector	ADSC QUANTUM 315r
Wavelength(s)	0.9801
Spacegroup name	P 21 21 2
Unit cell lengths	68.640, 63.060, 36.540
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	46.438 - 1.314
R-factor	0.1545
Rwork	0.153
R-free	0.19130
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4gql
RMSD bond length	0.006
RMSD bond angle	1.071
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	MOLREP
Refinement software	PHENIX (1.8_1069)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	46.438	1.350
High resolution limit [Å]	1.310	1.310
Rmerge	0.123	1.640
Number of reflections	71186
<I/σ(I)>	9.47	1.03
Completeness [%]	97.6	73.2
Redundancy	6.83	3.93

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	9.5	293	Protein : MMP12 F67D K241A, 1 mili-M + 10 mili-M AHA Drop : 1 micro-L protein + 0.2 micro-L inhibitor (5 mili-M in DMSO) Precipitant : 20% PEG4000, 0.2 M TRIS pH 9.5 Cryoprotectant : 10 % diethylene glycol + 5 % glycerol + 10 % 2,3-butanediol + 5 % 1,4-dioxane +25% PEG6000,+ 100 mili-M TRIS HCl, pH 8.