5C1T
Crystal structure of the GTP-bound wild type EhRabX3 from Entamoeba histolytica
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM14 |
| Synchrotron site | ESRF |
| Beamline | BM14 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2014-11-13 |
| Detector | MAR CCD 165 mm |
| Wavelength(s) | 0.97 |
| Spacegroup name | P 61 |
| Unit cell lengths | 62.965, 62.965, 312.021 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 44.692 - 2.801 |
| R-factor | 0.2665 |
| Rwork | 0.263 |
| R-free | 0.30210 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.150 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | PHENIX |
| Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 44.692 |
| High resolution limit [Å] | 2.800 |
| Number of reflections | 16942 |
| <I/σ(I)> | 12.5 |
| Completeness [%] | 98.9 |
| Redundancy | 7.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5 | 291 | 200mM Ammonium sulphate, 100mM BisTris, 25% PEG 3350 |
