3TVC

Human MMP13 in complex with L-glutamate motif 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	2011-06-13
Detector	ADSC QUANTUM 315r
Wavelength(s)	0.972420
Spacegroup name	P 21 21 2
Unit cell lengths	60.303, 85.160, 40.916
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	40.916 - 2.430
R-factor	0.1654
Rwork	0.162
R-free	0.23410
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3QJ2 catalytic domain only (Chain A)
RMSD bond length	0.008
RMSD bond angle	1.121
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	PHENIX ((phenix.refine))

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	85.100	85.100	2.590
High resolution limit [Å]	2.430	6.810	2.430
Rmerge	0.290	0.790	1.399
Number of reflections	8151
<I/σ(I)>	10.6	24.27	2.81
Completeness [%]	96.9	98	87.4
Redundancy	7.21	6.23	6.63

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	5.5	293	PROTEIN-INHIBITOR SOLUTION: MMP13 AT 20 MG/ML CO-CRYSTALLIZED WITH E3P AT 1.1 MILLI-M. RESERVOIR SOLUTION: 17.5% PEG 20K, 0.1 M MES, 0.02 M NACL. CRYOPROTECTANT: 5% DIETHYLENE GLYCOL, 5% ETHYLENE GLYCOL, 5% MPD, 5% PROPYLENE GLYCOL, 5% DMSO, 5% GLYCEROL, 0.005 M 3-(-PYRIDINIO)-1-PROPANESULFONATE, 10% PEG 20K, 0.033 M SODIUM ACETATE, 0.033 M ADA, 0.033 M BICINE, PH 5.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K