2IVS
Crystal structure of non-phosphorylated RET tyrosine kinase domain
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-4 |
Synchrotron site | ESRF |
Beamline | ID14-4 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2003-09-08 |
Detector | ADSC CCD |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 50.399, 80.217, 79.684 |
Unit cell angles | 90.00, 100.09, 90.00 |
Refinement procedure
Resolution | 50.000 - 2.000 |
R-factor | 0.183 |
Rwork | 0.180 |
R-free | 0.22900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1gjo |
RMSD bond length | 0.015 |
RMSD bond angle | 1.520 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | MOLREP |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 27.900 | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.080 | 0.250 |
Number of reflections | 41522 | |
<I/σ(I)> | 16 | 10 |
Completeness [%] | 97.5 | 80.6 |
Redundancy | 4 | 2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 295 | PROTEIN 3 MG/ML IN 20 MM TRIS-HCL PH 8.0, 10MM NACL, 1MM DTT RESERVOIR 2.0 M SODIUM FORMATE, 0.1M SODIUM CITRATE PH 5.5 VAPOUR DIFFUSION, SITTING DROP,295 K |