4H84

Crystal structure of the catalytic domain of Human MMP12 in complex with a selective carboxylate based inhibitor.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID23-1
Synchrotron site	ESRF
Beamline	ID23-1
Temperature [K]	100
Detector technology	CCD
Collection date	2012-06-14
Detector	ADSC QUANTUM 315r
Wavelength(s)	0.9763
Spacegroup name	P 21 21 21
Unit cell lengths	42.140, 62.790, 113.140
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	42.029 - 1.592
R-factor	0.1729
Rwork	0.171
R-free	0.20620
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4h30
RMSD bond length	0.007
RMSD bond angle	1.262
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	1.690
High resolution limit [Å]	1.590	4.750	1.590
Rmerge	0.159	0.070	0.957
Number of reflections	40489
<I/σ(I)>	10.64	23.58	3.13
Completeness [%]	98.6	95.7	92.6
Redundancy	7.68	6.24	7.47

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	293	Protein: hMMP12 F171D at4 784 mico-M + 10 milli-M AHA Reservoir: 12% PEG 20K, 0.14 M imidazole malate, .0175 M NaCl Cryoprotectant: 40% C7 (C7 = 12.5 % di-ethylene glycol + 12.5 % ethylene glycol + 25 % 1,2-propanediol + 12.5 % DMSO + 12.5 % glycerol), 1M NaCl, 0.1 M (MMT buffer 75% acid/25% basic), 9% PEG 10.000, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K