2XS3

Structure of karilysin catalytic MMP domain

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID23-2
Synchrotron site	ESRF
Beamline	ID23-2
Temperature [K]	100
Detector technology	CCD
Detector	MARRESEARCH
Spacegroup name	C 1 2 1
Unit cell lengths	121.370, 53.110, 86.300
Unit cell angles	90.00, 134.55, 90.00

Refinement procedure

Resolution	50.000 - 2.400
R-factor	0.19197
Rwork	0.189
R-free	0.25872
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1mnc
RMSD bond length	0.013
RMSD bond angle	1.321
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]	45.300	2.530
High resolution limit [Å]	2.400	2.400
Rmerge	0.090	0.510
Number of reflections	15411
<I/σ(I)>	14.8	2.5
Completeness [%]	99.3	95.9
Redundancy	4.1	3.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		293	CRYSTALLIZATION ASSAYS WERE PERFORMED BY THE SITTING-DROP VAPOR DIFFUSION METHOD. RESERVOIR SOLUTIONS WERE PREPARED BY A TECAN ROBOT AND CRYSTALLIZATION DROPS WERE DISPENSED ON 96X2-WELL MRC PLATES (INNOVADYNE) BY A CARTESIAN (GENOMIC SOLUTIONS) NANODROP ROBOT AT THE HIGH-THROUGHPUT CRYSTALLOGRAPHY PLATFORM AT BARCELONA SCIENCE PARK. CRYSTALS SUITABLE FOR STRUCTURE ANALYSIS WERE OBTAINED FOR UNBOUND KLY18 IN A BRUKER STEADY-TEMPERATURE CRYSTAL FARM AT 20C FROM DROPS CONTAINING 100NL OF PROTEIN SOLUTION (AT 9MG ML-1 IN 5MM TRIS-HCL, PH8.0, 0.02% SODIUM AZIDE) AND 100NL OF 45% 2-METHYL-2,4-PENTANEDIOL, 0.2M AMMONIUM ACETATE, 0.1M TRIS-HCL, PH8.5 AS RESERVOIR SOLUTION.