1Q1U
Crystal structure of human FHF1b (FGF12b)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X4A |
Synchrotron site | NSLS |
Beamline | X4A |
Temperature [K] | 90 |
Detector technology | CCD |
Collection date | 2002-10-30 |
Detector | ADSC QUANTUM 4 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 30.624, 58.853, 65.415 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 25.000 - 1.700 |
R-factor | 0.2231 |
Rwork | 0.223 |
R-free | 0.24000 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | PDB ID 1IHK |
RMSD bond length | 0.005 |
RMSD bond angle | 1.310 |
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 | 1.760 |
High resolution limit [Å] | 1.700 | 1.700 |
Rmerge | 0.058 * | 0.365 * |
Total number of observations | 93909 * | |
Number of reflections | 13171 | |
<I/σ(I)> | 7.03 | |
Completeness [%] | 97.0 | 85 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 20 * | 20% PEG 400, 200mM ammonium sulfate, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 45 (mg/ml) | |
2 | 1 | drop | HEPES | 25 (mM) | pH7.5 |
3 | 1 | drop | 300 (mM) | ||
4 | 1 | reservoir | PEG400 | 20-25 (%) | |
5 | 1 | reservoir | ammonium sulfate | 200 (mM) |