2F9L
3D structure of inactive human Rab11b GTPase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | LNLS BEAMLINE D03B-MX1 |
| Synchrotron site | LNLS |
| Beamline | D03B-MX1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2003-08-30 |
| Detector | MARRESEARCH |
| Wavelength(s) | 1.43 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 45.790, 52.218, 59.351 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 39.220 - 1.550 |
| R-factor | 0.18813 |
| Rwork | 0.186 |
| R-free | 0.23755 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1oiv |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.720 |
| Data reduction software | MOSFLM |
| Data scaling software | CCP4 ((SCALA)) |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 39.220 | 1.630 |
| High resolution limit [Å] | 1.550 | 1.550 |
| Number of reflections | 21134 | |
| <I/σ(I)> | 18.4 | 5 |
| Completeness [%] | 99.8 | 99.5 |
| Redundancy | 6.7 | 6.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.8 | 298 | Reservoir solution: 0.1M Tris-HCl pH8.8, 30% PEG 4000 Protein sample: 30 mg/ml Rab11b-GDP, 10mM Tris-HCl pH7.4, 0.1mM Mg Chloride , VAPOR DIFFUSION, HANGING DROP, temperature 298K |
