4H76

Crystal structure of the catalytic domain of Human MMP12 in complex with a broad spectrum hydroxamate 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	2011-01-31
Detector	ADSC QUANTUM 315r
Wavelength(s)	0.8726
Spacegroup name	P 21 21 2
Unit cell lengths	69.920, 62.890, 37.700
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	46.758 - 1.500
R-factor	0.1662
Rwork	0.165
R-free	0.18840
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3ljg
RMSD bond length	0.007
RMSD bond angle	1.079
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	0.114	0.044	1.094
Number of reflections	27420
<I/σ(I)>	14.21	40.9	2.5
Completeness [%]	99.7
Redundancy	7.98	7.13	7.92

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	293	Protein:(hMMP12 F171D at 927 micro-M + acetohydroxamic acid at 11.6 milli-M Reservoir: 45% PEG 4,000 0.2 M imidazole piperidine Cryoprotection: 10% Di-ethylene glycol, 10% 1.2-propanediol, 10% glycerol, 10% PEG 10,000, 10% (AAB buffer 10% acid/90% basic) 0.2 M NaCl. Flash cooling in LN2. , pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K