1OIV
X-ray structure of the small G protein Rab11a in complex with GDP
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-1 |
| Synchrotron site | ESRF |
| Beamline | ID14-1 |
| Temperature [K] | 100 |
| Collection date | 2001-11-11 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 47.349, 69.701, 108.277 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 * - 1.980 |
| R-factor | 0.21 |
| Rwork | 0.210 |
| R-free | 0.24600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1g16 |
| RMSD bond length | 0.005 |
| RMSD bond angle | 22.500 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 * | 1.980 |
| High resolution limit [Å] | 1.950 | 1.950 |
| Rmerge | 0.049 | 0.393 |
| Total number of observations | 233617 * | |
| Number of reflections | 26100 * | |
| <I/σ(I)> | 9 | |
| Completeness [%] | 97.2 | 97.4 |
| Redundancy | 5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion * | 8 | 20 * | 1.7M (NH4)2SO4,5%PEG400,8% 1,3 BUTANEDIOL,0.1M TRIS-HCL PH8.0, pH 8.00 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | |
| 2 | 1 | reservoir | ammonium sulfate | 1.6-1.8 (M) | |
| 3 | 1 | reservoir | PEG400 | 3-6 (%) | |
| 4 | 1 | reservoir | 1,3-butanediol | 3-10 (%) | |
| 5 | 1 | reservoir | Tris-HCl | 100 (mM) | pH8-8.5 |
