2XS4

Structure of karilysin catalytic MMP domain in complex with magnesium

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID29
Synchrotron site	ESRF
Beamline	ID29
Temperature [K]	100
Detector technology	CCD
Detector	ADSC CCD
Spacegroup name	I 4
Unit cell lengths	85.790, 85.790, 53.480
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	50.000 - 1.700
R-factor	0.15878
Rwork	0.158
R-free	0.18575
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2xs3
RMSD bond length	0.006
RMSD bond angle	1.034
Data reduction software	XDS
Data scaling software	SCALA
Phasing software	PHASER
Refinement software	REFMAC (5.5.0102)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.300	1.790
High resolution limit [Å]	1.700	1.700
Rmerge	0.030	0.120
Number of reflections	21225
<I/σ(I)>	37.1	10.8
Completeness [%]	99.0	95.9
Redundancy	7.2	4.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1			277	CRYSTALS OF MAGNESIUM-BOUND KLY18 WERE OBTAINED AT 4C BY MIXING PROTEIN SOLUTION PREINCUBATED WITH CALCIUM (AT 7.3MG ML-1 IN 5MM TRIS-HCL, PH8.0, 5MM CALCIUM CHLORIDE, 0.02% SODIUM AZIDE) AND 14% SODIUM POLYACRYLATE 5100, 20MM MAGNESIUM CHLORIDE, 0.1M HEPES, PH7.5 IN A VOLUME RATIO OF 1:3. THE LATTER CONDITIONS WERE SCALED UP TO THE MICROLITER RANGE WITH 24-WELL CRYSCHEM CRYSTALLIZATION DISHES (HAMPTON RESEARCH).