4H3X

Crystal structure of an MMP broad spectrum hydroxamate based inhibitor CC27 in complex with the MMP-9 catalytic domain

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 1 21 1
Unit cell lengths	40.110, 97.940, 46.080
Unit cell angles	90.00, 111.73, 90.00

Refinement procedure

Resolution	42.806 - 1.764
R-factor	0.1993
Rwork	0.196
R-free	0.25410
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4h2e
RMSD bond length	0.007
RMSD bond angle	1.030
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	1.870
High resolution limit [Å]	1.760	5.260	1.760
Rmerge	0.136	0.073	0.666
Number of reflections	31957
<I/σ(I)>	8.41	18.06	2.33
Completeness [%]	98.0	99	94.2
Redundancy	4.23	4.13	4.13

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7	293	protein: hMMP-9-WT 5.5 mg/mL 120 milli-M acetohydroxamic acid. Reservoir: 10% PEG 20,000, 60mM MES pH 5.5 + 18% MPEG 5,000, 0.08 M imidazole piperidine; pH 8.5, 0.05 M NaCl. Cryoprotectant: 10% Di-ethylene glycol, 10% 1.2-propanediol, 10% glycerol, 10% PEG 10K, 10% PCTP 50/50, 200mM NaCl , VAPOR DIFFUSION, SITTING DROP, temperature 293K