4FVL

Human collagenase 3 (MMP-13) full form with peptides from pro-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	CCD
Collection date	2010-12-20
Detector	ADSC QUANTUM 315r
Wavelength(s)	0.980110
Spacegroup name	C 2 2 21
Unit cell lengths	125.780, 157.270, 105.550
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	49.114 - 2.436
R-factor	0.1685
Rwork	0.166
R-free	0.22300
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4fu4
RMSD bond length	0.009
RMSD bond angle	1.196
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	2.580
High resolution limit [Å]	2.440	7.240	2.440
Rmerge	0.165	0.053	1.025
Number of reflections	37803
<I/σ(I)>	11.15	26.79	2.71
Completeness [%]	95.7	88.8	96.6
Redundancy	5.82	5.46	5.69

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	SLOW COOLING	7.5	277	propeptide impurity induces crystallization on cold storage cryoprotectant: 10% Di-ethylene glycol, 10% 1.2-propanediol, 10% glycerol, 10% PEG 10K, 10% PCTP 80/20, 0.2 M NaCl, pH 7.5, SLOW COOLING, temperature 277.0K