5CZM

Crystal structure of a mutated catalytic domain of Human MMP12 in complex with 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	2015-07-12
Detector	ADSC QUANTUM 315r
Wavelength(s)	0.9184
Spacegroup name	P 21 21 2
Unit cell lengths	68.970, 63.290, 35.910
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	28.451 - 1.303
R-factor	0.1468
Rwork	0.145
R-free	0.17390
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4gql
RMSD bond length	0.006
RMSD bond angle	1.057
Data reduction software	XDS
Data scaling software	XDS
Phasing software	MOLREP
Refinement software	PHENIX (1.8_1069)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	46.632	1.380
High resolution limit [Å]	1.300	1.300
Rmerge	0.207	2.097
Number of reflections	74004
<I/σ(I)>	9.96	1.1
Completeness [%]	99.6	97.5
Redundancy	6.5	6.14

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	9.5	293	Protein : MMP12h F67D K241A 850 micro-M + 10mM AHA Drop : 1 micro-L protein + 0.35 micro-l inhibitor(1.5 milli-M, DMSO) Precipitant : 20% PEG4K, 0.2 M TRIS pH9.5 Cryo protectant : 5% diethylene glycol, 0% ethylene glycol, 5% MPD + 5% glycerol, 5% 2,3-butanediol, 5mM NDSB 201, 25% PEG 6K, 100mM TRIS HCl, pH 8.0