2XIR

Crystal structure of the VEGFR2 kinase domain in complex with PF- 00337210 (N,2-dimethyl-6-(7-(2-morpholinoethoxy)quinolin-4-yloxy) benzofuran-3-carboxamide)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 5.0.2
Synchrotron site	ALS
Beamline	5.0.2
Temperature [K]	89
Detector technology	CCD
Collection date	2004-08-04
Detector	ADSC CCD
Spacegroup name	C 1 2 1
Unit cell lengths	135.267, 56.827, 52.187
Unit cell angles	90.00, 94.18, 90.00

Refinement procedure

Resolution	19.920 - 1.500
R-factor	0.21852
Rwork	0.217
R-free	0.23808
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1vr2
RMSD bond length	0.006
RMSD bond angle	1.091
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	MOLREP
Refinement software	REFMAC (5.2.0019)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	1.500
High resolution limit [Å]	1.450	1.450
Rmerge	0.060	0.480
Number of reflections	67226
<I/σ(I)>	22	1.22
Completeness [%]	95.8	68.2
Redundancy	4.4	2.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	286	PROTEIN PRODUCTION, PROTEIN PURIFICATION, AND COCRYSTALLIZATION WERE PERFORMED AS PREVIOUSLY DESCRIBED (PUBLISHED INTERNATIONAL PATENT APPLICATION WO 2004/092217 HANGING DROP VAPOR DIFFUSION AT 13 DEGREES C. 2 MICROLITERS OF A 7.7 MG/ML PROTEIN SOLUTION (IN 50 MM HEPES 7.5, 30 MM SODIUM CHLORIDE, 5 MM DTT, AND 5% DMSO) WAS MIXED WITH 2 MICROLITERS OF CRYSTALLIZATION SOLUTION (100 MM HEPES PH 7.5, 20% PEG 6K AND 5% MPD) AND SUSPENDED OVER 1 ML OF CRYSTALLIZATION SOLUTION PLUS 5 MICROLITERS BME.