1NUN
Crystal Structure Analysis of the FGF10-FGFR2b Complex
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X4A |
Synchrotron site | NSLS |
Beamline | X4A |
Temperature [K] | 90 |
Detector technology | CCD |
Collection date | 2001-11-15 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 0.97880, 0.97933, 0.97169 |
Spacegroup name | P 64 2 2 |
Unit cell lengths | 113.930, 113.930, 164.852 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 25.000 - 2.900 |
R-factor | 0.232 |
Rwork | 0.239 |
R-free | 0.28800 |
Structure solution method | MAD |
RMSD bond length | 0.008 * |
RMSD bond angle | 1.400 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS (1.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 25.000 | 3.140 |
High resolution limit [Å] | 2.900 | 2.900 |
Rmerge | 0.064 * | 0.279 * |
Total number of observations | 279164 * | |
Number of reflections | 14520 * | |
Completeness [%] | 99.3 | 100 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 * | 20 * | PEG 400, ammonium sulfate, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | PEG400 | 3 (%) | |
2 | 1 | reservoir | ammonium sulfate | 2.0 (M) | |
3 | 1 | reservoir | Tris-HCl | 0.1 (M) | pH8.5 |
4 | 1 | drop | protein | 7 (mg/ml) | |
5 | 1 | drop | HEPES | 25 (mM) | pH7.5 |
6 | 1 | drop | 150 (mM) |