4HMA

Crystal structure of an MMP twin carboxylate based inhibitor LC20 in complex with the MMP-9 catalytic domain

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SOLEIL BEAMLINE PROXIMA 1
Synchrotron site	SOLEIL
Beamline	PROXIMA 1
Temperature [K]	100
Detector technology	PIXEL
Collection date	2012-10-12
Detector	PSI PILATUS 6M
Wavelength(s)	0.98011
Spacegroup name	P 21 21 2
Unit cell lengths	73.870, 98.240, 47.440
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	42.720 - 1.940
R-factor	0.21439
Rwork	0.211
R-free	0.28302
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4h82
RMSD bond length	0.022
RMSD bond angle	1.966
Data reduction software	XDS
Data scaling software	XDS
Phasing software	MOLREP
Refinement software	REFMAC (5.5.0109)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	2.060
High resolution limit [Å]	1.940	5.790	1.940
Rmerge	0.166	0.056	1.533
Number of reflections	26019
<I/σ(I)>	8.19	23.21	1.3
Completeness [%]	99.4	99.5	96.6
Redundancy	7.98	7.15	7.87

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6	293	Protein: human MMP9 (E402Q) at 308.7 micro-M twin inhibitor LC20 at 154 micro-M (stoichiometry 2:1) and 120mM acetohydroxamic acid. RESERVOIR: 12% Polyethylene glycol 20,000, 1.5M NaCl, 0.1 M PCTP (Na propionate, Na cacodylate, Bis-Tris-propane ratio 2:1:2; 75% pH 4, 25% pH 9.5) CRYOPROTECTANT: 40% C2 (25 % di-ethylene glycol + 25 % glycerol + 25 % 1,2-propanediol), 9% PEG 10,000 1.5M NaCl, 0.1M PCTP 80/2, VAPOR DIFFUSION, SITTING DROP, temperature 293K