1II4
CRYSTAL STRUCTURE OF SER252TRP APERT MUTANT FGF RECEPTOR 2 (FGFR2) IN COMPLEX WITH FGF2
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2000-08-26 |
Detector | RIGAKU RAXIS IIC |
Wavelength(s) | 1.5418 |
Spacegroup name | P 1 |
Unit cell lengths | 70.970, 72.657, 89.739 |
Unit cell angles | 89.98, 89.70, 90.00 |
Refinement procedure
Resolution | 25.000 - 2.700 |
R-factor | 0.238 |
Rwork | 0.238 |
R-free | 0.26700 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1ev2 |
RMSD bond length | 0.008 |
RMSD bond angle | 1.400 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.800 |
High resolution limit [Å] | 2.700 | 2.700 |
Rmerge | 0.050 | 0.250 |
Total number of observations | 74426 * | |
Number of reflections | 46770 * | |
<I/σ(I)> | 12.1 | |
Completeness [%] | 91.6 | 79.7 |
Redundancy | 1.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 7.5 | 298 | PEG 4000, Isopropanol, HEPES-NaOH, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10 (mg/ml) | |
2 | 1 | drop | HEPES-NaOH | 25 (mM) | |
3 | 1 | drop | 150 (mM) | ||
4 | 1 | reservoir | PEG4000 | 10-15 (%) | |
5 | 1 | reservoir | isopropanol alcohol | 10 (%) | |
6 | 1 | reservoir | HEPES-NaOH | 0.1 (M) |