2WGJ
X-ray Structure of PF-02341066 bound to the kinase domain of c-Met
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] | 95 |
Detector technology | CCD |
Collection date | 2006-04-30 |
Detector | ADSC CCD |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 76.926, 94.192, 45.990 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 19.960 - 2.000 |
R-factor | 0.21485 |
Rwork | 0.214 |
R-free | 0.23153 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3lck |
RMSD bond length | 0.008 |
RMSD bond angle | 1.081 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | EPMR |
Refinement software | REFMAC (5.1.24) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.050 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.060 | 0.290 |
Number of reflections | 18192 | |
<I/σ(I)> | 20 | 2.5 |
Completeness [%] | 78.1 | 38.5 |
Redundancy | 3.9 | 2.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 4.6 | 286 | CRYSTALS WERE GROWN BY HANGING DROP VAPOR DIFFUSION AT 13 DEGREES CELCIUS. 1-2 MICROLITERS OF PROTEIN SOLUTION AT 7-15 MG/ML WAS MIXEDWITH AN EQUAL VOLUME OF PRECIPITATING SOLUTION (0-275 MM SODIUM CHLORIDE, 21% (W/V PEG 3350, 50 MM CITRATE-PHOSPHATE PH 4.6) |