4FU4

Human collagenase 3 (MMP-13) with peptide from pro-domain

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-4
Synchrotron site	ESRF
Beamline	ID14-4
Temperature [K]	100
Detector technology	CCD
Collection date	2009-07-01
Detector	ADSC QUANTUM 4r
Wavelength(s)	0.9395
Spacegroup name	C 2 2 21
Unit cell lengths	127.080, 156.580, 106.140
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	49.336 - 2.849
R-factor	0.1816
Rwork	0.178
R-free	0.24680
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1PEX AND 2OW9
RMSD bond length	0.009
RMSD bond angle	1.264
Data reduction software	XDS
Data scaling software	XSCALE
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	3.020
High resolution limit [Å]	2.850	8.440	2.850
Rmerge	0.170	0.044	0.712
Number of reflections	25083
<I/σ(I)>	13.88	37.05	3.24
Completeness [%]	99.8	99.3	99
Redundancy	7.78	6.73	8.23

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	SLOW COOLING	7.5	277	PROPEPTIDE IMPURITY INDUCES CRYSTALLIZATION ON COLD STORAGE CRYOPROTECTANT: 20% MPEG2K, 10% MPEG550, 10% ethylene glycol, 90mM imidazole malate, pH 6.0, SLOW COOLING, temperature 277.0K