4H1Q

Crystal structure of mutant MMP-9 catalytic domain in complex with a twin inhibitor.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-1
Synchrotron site	ESRF
Beamline	ID14-1
Temperature [K]	100
Detector technology	CCD
Collection date	2010-11-24
Detector	ADSC QUANTUM 4r
Spacegroup name	P 1 21 1
Unit cell lengths	44.140, 48.660, 67.920
Unit cell angles	90.00, 102.55, 90.00

Refinement procedure

Resolution	43.090 - 1.590
R-factor	0.172
Rwork	0.170
R-free	0.21100
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2ow1
RMSD bond length	0.008
RMSD bond angle	1.472
Data reduction software	XDS
Data scaling software	XDS
Phasing software	MOLREP
Refinement software	PHENIX ((phenix.refine: 1.8_1069))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	1.680
High resolution limit [Å]	1.590	1.590
Rmerge	0.012	1.229
Number of reflections	36921
<I/σ(I)>	11.53	1.35
Completeness [%]	96.8	94.7
Redundancy	4.3	4.06

Crystallization Conditions

crystal ID	method	pH	temperature	details
1		8	293	Protein: MMP9h Nter=GFQT E402Q V391Q at 130.3 micro-M with 5 milli-M AHA Reservoir: 40% MPEG 5K, 100mM HEPES. Cryoprotectant: 35% MPEG 5K, 15% PEG 400, 15% AAB (90/10), pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K