5I12

Crystal structure of the catalytic domain of MMP-9 in complex with a selective sugar-conjugated arylsulfonamide carboxylate water-soluble inhibitor (DC27).

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID23-2
Synchrotron site	ESRF
Beamline	ID23-2
Temperature [K]	100
Detector technology	PIXEL
Collection date	2014-06-19
Detector	DECTRIS PILATUS 2M
Wavelength(s)	0.8729
Spacegroup name	P 32 2 1
Unit cell lengths	39.560, 39.560, 163.550
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	34.260 - 1.590
R-factor	0.19
Rwork	0.188
R-free	0.22800
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4h3x
RMSD bond length	0.006
RMSD bond angle	1.033
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	MOLREP
Refinement software	PHENIX (1.9_1692)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	35.000	1.630
High resolution limit [Å]	1.590	1.590
Rmerge	0.115	1.630
Number of reflections	20981
<I/σ(I)>	15.04	1.65
Completeness [%]	99.7	96.8
Redundancy	13.2	13.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.25	293	protein solution: 415.2 micro-M MMP9 WT + 0.120 M Acetohydroxamic acid in 20 mM Tris pH 7.0 with 0.001 M inhibitor DC27 and 10% DMSO. precipitant: 40% MPEG 5K ; 0.1 M bicine ; pH 7.25 sitting drops of 1 micro-L protein solution and 1 micro-L precipitant solution. cryoprotectant:_40% cryomix CM2 (25 % di-ethylene glycol + 25 % glycerol + 25 % 1,2-propanediol), 10% PEG 10K, 200 milli-M NaCl, 100 milli-M Na propionate, Na cacodylate, Bis-Tris-propane (PCTP 50% acid/50% basic) pH 7.0 + 0.001 M inhibitor DC27.