2VXT

Crystal structure of human IL-18 complexed to murine reference antibody 125-2H Fab

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 32-ID
Synchrotron site	APS
Beamline	32-ID
Temperature [K]	100
Detector technology	CCD
Collection date	2003-04-29
Detector	MARRESEARCH
Spacegroup name	P 1 21 1
Unit cell lengths	44.345, 62.435, 104.734
Unit cell angles	90.00, 100.39, 90.00

Refinement procedure

Resolution	31.160 - 1.490
R-factor	0.164
Rwork	0.162
R-free	0.19600
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1fns
RMSD bond length	0.012
RMSD bond angle	1.662
Data reduction software	HKL-2000
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	REFMAC (5.2.0019)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	1.540
High resolution limit [Å]	1.490	1.490
Rmerge	0.060	0.350
Number of reflections	86865
<I/σ(I)>	10.4	2.3
Completeness [%]	94.8	56.6
Redundancy	3.5	2.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8.5	277	IL-18 AND 125-2H FAB WERE MIXED (1:3 MASS RATIO), INCUBATED OVERNIGHT AT 277 K, PURIFIED BY MONOQ ANION EXCHANGE CHROMATOGRAPHY, AND CONCENTRATED TO 10 MG/ML. THE COMPLEX WAS CRYSTALLIZED BY HANGING DROP VAPOR DIFFUSION BY MIXING COMPLEX (1.5 MICROLITERS [UL]) WITH 1.8 UL OF RESERVOIR SOLUTION (30% PEG 4000, 100 MM TRIS, PH 8.5, 0.2 M MGCL2) AND 0.3 UL OF 300 MM SULFO-BETAINE 201, AND SUSPENDING THE DROP OVER THE RESERVOIR AT 291 K. ROD-LIKE CRYSTALS APPEARED WITHIN ONE WEEK.