1FST
CRYSTAL STRUCTURE OF TRUNCATED HUMAN RHOGDI TRIPLE MUTANT
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | EMBL/DESY, HAMBURG BEAMLINE X11 |
Synchrotron site | EMBL/DESY, HAMBURG |
Beamline | X11 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 1999-12-06 |
Detector | MAR CCD 165 mm |
Spacegroup name | H 3 |
Unit cell lengths | 125.210, 125.210, 82.660 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 20.000 - 2.700 |
Rwork | 0.213 |
R-free | 0.26100 |
RMSD bond length | 0.007 |
RMSD bond angle | 25.800 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS (0.9) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.780 |
High resolution limit [Å] | 2.700 | 2.700 |
Rmerge | 0.048 | 0.267 |
Total number of observations | 49713 * | |
Number of reflections | 13241 | |
<I/σ(I)> | 17.9 | |
Completeness [%] | 99.6 | 99.6 |
Redundancy | 3.8 | 3.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 7 | 293 | PEG 3400, isopropanol, HEPES buffer, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 7-15 (mg/ml) | |
2 | 1 | reservoir | PEG3400 | 12-14 (%) | |
3 | 1 | reservoir | 2-propanol | 5 (%) | |
4 | 1 | reservoir | HEPES | 100 (mM) |