4LHV
Crystal structure of Rab8 in its inactive GDP-bound form
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X10SA |
| Synchrotron site | SLS |
| Beamline | X10SA |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-05-01 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.9786 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 117.836, 75.950, 106.618 |
| Unit cell angles | 90.00, 98.44, 90.00 |
Refinement procedure
| Resolution | 19.960 - 1.950 |
| R-factor | 0.20441 |
| Rwork | 0.202 |
| R-free | 0.24428 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1yzq |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.354 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALEPACK |
| Phasing software | PHASES |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 20.000 |
| High resolution limit [Å] | 1.950 |
| Number of reflections | 67378 |
| Completeness [%] | 99.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 293 | All crystals were obtained by mixing 1 ul protein and 1 ul reservoir solution. Crystals of Rab8a6-176:GDP were obtained by mixing of 1 ul protein (20 mg/ml, buffer: 25 mM HEPES pH 7.5, 40 mM NaCl, 1 mM MgCl2, 10 M GDP and 5 mM beta-mercaptoethanol) with 1 ul of reservoir consisting of 16% (w/v) PEG4000, 0.1 M CaAc2, 0.1 M HEPES. The crystal was protected with cryo solution containing 30% (w/v) PEG4000, 0.1 M CaAc2, 0.1 M HEPES pH 7.0 before data collection, VAPOR DIFFUSION, HANGING DROP, temperature 293K |






