1EV2
CRYSTAL STRUCTURE OF FGF2 IN COMPLEX WITH THE EXTRACELLULAR LIGAND BINDING DOMAIN OF FGF RECEPTOR 2 (FGFR2)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X4A |
Synchrotron site | NSLS |
Beamline | X4A |
Temperature [K] | 110 |
Detector technology | AREA DETECTOR |
Collection date | 1999-09-22 |
Detector | SDMS |
Spacegroup name | P 1 |
Unit cell lengths | 72.198, 71.677, 90.920 |
Unit cell angles | 90.53, 89.98, 89.99 |
Refinement procedure
Resolution | 25.000 - 2.200 |
R-factor | 0.248 |
Rwork | 0.248 |
R-free | 0.27300 |
RMSD bond length | 0.007 |
RMSD bond angle | 0.782 * |
Data reduction software | SDMS |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 25.000 | 2.280 |
High resolution limit [Å] | 2.200 | 2.200 |
Rmerge | 0.042 | 0.241 |
Total number of observations | 206913 * | |
Number of reflections | 93440 * | |
<I/σ(I)> | 16.3 | |
Completeness [%] | 96.3 | 87.8 |
Redundancy | 2.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7.5 | 298 | drop consists of equal volume of protein and reservoir solutions * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10 (mg/ml) | |
2 | 1 | drop | Tris-HCl | 25 (mM) | |
3 | 1 | drop | 150 (mM) | ||
4 | 1 | reservoir | PEG4000 | 10-15 (%) | |
5 | 1 | reservoir | isopropanol | 10 (%) | |
6 | 1 | reservoir | HEPES-NaOH | 0.1 (M) |