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. |